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Volumn 10, Issue 1, 1998, Pages 93-101

Intermediate filaments and their associated proteins: Multiple dynamic personalities

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN;

EID: 0032006027     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(98)80091-4     Document Type: Article
Times cited : (54)

References (60)
  • 1
    • 0029795964 scopus 로고    scopus 로고
    • The function of intermediate filaments in cell shape and cytoskeletal integrity
    • of outstanding interest. The use of injected intermediate filament (IF) mimetic peptides that rapidly disrupt all three filamentous networks of the cytoskeleton suggests a central role for filaments in maintaining cellular architecture and hints that IF-associated proteins may act as adaptors between the different network types.
    • Goldman RD, Khuon S, Chou YH, Opal P, Steinert PM. The function of intermediate filaments in cell shape and cytoskeletal integrity. of outstanding interest J Cell Biol. 134:1996;971-983 The use of injected intermediate filament (IF) mimetic peptides that rapidly disrupt all three filamentous networks of the cytoskeleton suggests a central role for filaments in maintaining cellular architecture and hints that IF-associated proteins may act as adaptors between the different network types.
    • (1996) J Cell Biol , vol.134 , pp. 971-983
    • Goldman, R.D.1    Khuon, S.2    Chou, Y.H.3    Opal, P.4    Steinert, P.M.5
  • 2
    • 0030717391 scopus 로고    scopus 로고
    • To bead or not to bead? Lens specific intermediate filaments revisited
    • of special interest. This thorough discussion of lens-specific beaded intermediate filaments (IFs) describes the current state of the field and highlights the work that led to our present understanding of this distinct class of IFs.
    • Georgatos SD, Gounari F, Goulielmos G, Aebi U. To bead or not to bead? Lens specific intermediate filaments revisited. of special interest J Cell Sci. 110:1997;2629-2634 This thorough discussion of lens-specific beaded intermediate filaments (IFs) describes the current state of the field and highlights the work that led to our present understanding of this distinct class of IFs.
    • (1997) J Cell Sci , vol.110 , pp. 2629-2634
    • Georgatos, S.D.1    Gounari, F.2    Goulielmos, G.3    Aebi, U.4
  • 3
    • 0023840076 scopus 로고
    • Cytoskeleton-associated plectin: In situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins
    • Foisner R, Leichtfried FE, Herrmann H, Small JV, Lawson D, Wiche G. Cytoskeleton-associated plectin: in situ localization, in vitro reconstitution, and binding to immobilized intermediate filament proteins. J Cell Biol. 106:1988;723-733.
    • (1988) J Cell Biol , vol.106 , pp. 723-733
    • Foisner, R.1    Leichtfried, F.E.2    Herrmann, H.3    Small, J.V.4    Lawson, D.5    Wiche, G.6
  • 4
    • 0025797361 scopus 로고
    • Protein kinase A- And protein kinase C-regulated interaction of plectin with lamin B and vimentin
    • Foisner R, Traub P, Wiche G. Protein kinase A- and protein kinase C-regulated interaction of plectin with lamin B and vimentin. Proc Natl Acad Sci USA. 88:1991;3812-3816.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 3812-3816
    • Foisner, R.1    Traub, P.2    Wiche, G.3
  • 5
    • 0029805514 scopus 로고    scopus 로고
    • Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton
    • of outstanding interest. The immunoelectron microscopy images presented in this work convincingly document the association of plectin with multiple cellular partners (intermediate filaments, microtubules, actin filaments, and myosin), confirming previous biochemical data and establishing plectin as a true organizer of intracellular space.
    • Svitkina TM, Verkhovsky AB, Borisy GG. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. of outstanding interest J Cell Biol. 135:1996;991-1007 The immunoelectron microscopy images presented in this work convincingly document the association of plectin with multiple cellular partners (intermediate filaments, microtubules, actin filaments, and myosin), confirming previous biochemical data and establishing plectin as a true organizer of intracellular space.
    • (1996) J Cell Biol , vol.135 , pp. 991-1007
    • Svitkina, T.M.1    Verkhovsky, A.B.2    Borisy, G.G.3
  • 6
    • 10144233447 scopus 로고    scopus 로고
    • Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions
    • Nikolic B, Mac Nulty E, Mir B, Wiche G. Basic amino acid residue cluster within nuclear targeting sequence motif is essential for cytoplasmic plectin-vimentin network junctions. J Cell Biol. 134:1996;1455-1467.
    • (1996) J Cell Biol , vol.134 , pp. 1455-1467
    • Nikolic, B.1    Mac Nulty, E.2    Mir, B.3    Wiche, G.4
  • 7
    • 0030598838 scopus 로고    scopus 로고
    • An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments
    • of outstanding interest. The discovery that the neuronal protein BPAG1n/dystonin can co-align neurofilaments with actin filaments in cultured cells strengthens its claim as a cytoskeletal cross-linking protein and provides an explanation for the defects seen in mice disrupted in this locus (see also [18]).
    • Yang Y, Dowling J, Yu QC, Kouklis P, Cleveland DW, Fuchs E. An essential cytoskeletal linker protein connecting actin microfilaments to intermediate filaments. of outstanding interest Cell. 86:1996;655-665 The discovery that the neuronal protein BPAG1n/dystonin can co-align neurofilaments with actin filaments in cultured cells strengthens its claim as a cytoskeletal cross-linking protein and provides an explanation for the defects seen in mice disrupted in this locus (see also [18]).
    • (1996) Cell , vol.86 , pp. 655-665
    • Yang, Y.1    Dowling, J.2    Yu, Q.C.3    Kouklis, P.4    Cleveland, D.W.5    Fuchs, E.6
  • 8
    • 0030020359 scopus 로고    scopus 로고
    • M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase
    • of special interest. The identification of a kinase responsible for the redistribution of the cross-linking protein plectin from an insoluble vimentin-bound state in interphase cells to a more soluble vimentin-independent state during mitosis strongly suggests that plectin acts to modulate cell architecture in many stages of the cell cycle.
    • Foisner R, Malecz N, Dressel N, Stadler C, Wiche G. M-phase-specific phosphorylation and structural rearrangement of the cytoplasmic cross-linking protein plectin involve p34cdc2 kinase. of special interest Mol Biol Cell. 7:1996;273-288 The identification of a kinase responsible for the redistribution of the cross-linking protein plectin from an insoluble vimentin-bound state in interphase cells to a more soluble vimentin-independent state during mitosis strongly suggests that plectin acts to modulate cell architecture in many stages of the cell cycle.
    • (1996) Mol Biol Cell , vol.7 , pp. 273-288
    • Foisner, R.1    Malecz, N.2    Dressel, N.3    Stadler, C.4    Wiche, G.5
  • 9
    • 0031127727 scopus 로고    scopus 로고
    • Dynamic organization of intermediate filaments and associated proteins during the cell cycle
    • Foisner R. Dynamic organization of intermediate filaments and associated proteins during the cell cycle. Bioessays. 17:1997;297-305.
    • (1997) Bioessays , vol.17 , pp. 297-305
    • Foisner, R.1
  • 10
    • 0029961661 scopus 로고    scopus 로고
    • Human plectin: Organization of the gene, sequence analysis, and chromosome localization (8q24)
    • Liu CG, Maercker C, Castanon MJ, Hauptmann R, Wiche G. Human plectin: organization of the gene, sequence analysis, and chromosome localization (8q24). Proc Natl Acad Sci USA. 93:1996;4278-4283.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4278-4283
    • Liu, C.G.1    Maercker, C.2    Castanon, M.J.3    Hauptmann, R.4    Wiche, G.5
  • 11
    • 0030588594 scopus 로고    scopus 로고
    • Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins
    • of special interest. This preliminary characterization of the newest plakin family member, mACF7, reveals that the three mACF7 isoforms have considerable homology to BPAG1n/dystonin and also contain actin binding domain regions. It seems likely that this is the first of many such linking proteins to be found using homology with other proteins known to connect intermediate filaments to other cytoskeletal components.
    • Bernier G, Mathieu M, de Repentigny Y, Vidal SM, Kothary R. Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins. of special interest Genomics. 38:1996;19-29 This preliminary characterization of the newest plakin family member, mACF7, reveals that the three mACF7 isoforms have considerable homology to BPAG1n/dystonin and also contain actin binding domain regions. It seems likely that this is the first of many such linking proteins to be found using homology with other proteins known to connect intermediate filaments to other cytoskeletal components.
    • (1996) Genomics , vol.38 , pp. 19-29
    • Bernier, G.1    Mathieu, M.2    De Repentigny, Y.3    Vidal, S.M.4    Kothary, R.5
  • 12
    • 0030795164 scopus 로고    scopus 로고
    • The plakin family: Versatile organizers of cytoskeletal architecture
    • Ruhrberg C, Watt FM. The plakin family: versatile organizers of cytoskeletal architecture. Curr Opin Genet Dev. 7:1997;392-397.
    • (1997) Curr Opin Genet Dev , vol.7 , pp. 392-397
    • Ruhrberg, C.1    Watt, F.M.2
  • 13
    • 9344248374 scopus 로고    scopus 로고
    • Plectin deficiency results in muscular dystrophy with epidermolysis bullosa
    • of outstanding interest. The demonstration that mutations in a cytoskeletal linker protein such as plectin can cause a human disease characterized by a lack of cell integrity was a clear indication of plectin's essential function in different cell types and argued strongly for the importance of other linker proteins. See also [14-16].
    • Smith FJ, Eady RA, Leigh IM, McMillan JR, Rugg EL, Kelsell DP, Bryant SP, Spurr NK, Geddes JF, Kirtschig G, et al. Plectin deficiency results in muscular dystrophy with epidermolysis bullosa. of outstanding interest Nat Genet. 13:1996;450-457 The demonstration that mutations in a cytoskeletal linker protein such as plectin can cause a human disease characterized by a lack of cell integrity was a clear indication of plectin's essential function in different cell types and argued strongly for the importance of other linker proteins. See also [14-16].
    • (1996) Nat Genet , vol.13 , pp. 450-457
    • Smith, F.J.1    Eady, R.A.2    Leigh, I.M.3    McMillan, J.R.4    Rugg, E.L.5    Kelsell, D.P.6    Bryant, S.P.7    Spurr, N.K.8    Geddes, J.F.9    Kirtschig, G.10
  • 14
    • 9444272226 scopus 로고    scopus 로고
    • Loss of plectin causes epidermolysis bullosa with muscular dystrophy: CDNA cloning and genomic organization
    • of outstanding interest. The demonstration that mutations in a cytoskeletal linker protein such as plectin can cause a human disease characterized by a lack of cell integrity was a clear indication of plectin's essential function in different cell types and argued strongly for the importance of other linker proteins. See also [13,15,16].
    • McLean WH, Pulkkinen L, Smith FJ, Rugg EL, Lane EB, Bullrich F, Burgeson RE, Amano S, Hudson DL, Owaribe K, et al. Loss of plectin causes epidermolysis bullosa with muscular dystrophy: cDNA cloning and genomic organization. of outstanding interest Genes Dev. 10:1996;1724-1735 The demonstration that mutations in a cytoskeletal linker protein such as plectin can cause a human disease characterized by a lack of cell integrity was a clear indication of plectin's essential function in different cell types and argued strongly for the importance of other linker proteins. See also [13,15,16].
    • (1996) Genes Dev , vol.10 , pp. 1724-1735
    • McLean, W.H.1    Pulkkinen, L.2    Smith, F.J.3    Rugg, E.L.4    Lane, E.B.5    Bullrich, F.6    Burgeson, R.E.7    Amano, S.8    Hudson, D.L.9    Owaribe, K.10
  • 15
    • 0029798270 scopus 로고    scopus 로고
    • Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy
    • of outstanding interest. The demonstration that mutations in a cytoskeletal linker protein such as plectin can cause a human disease characterized by a lack of cell integrity was a clear indication of plectin's essential function in different cell types and argued strongly for the importance of other linker proteins. See also [13,14,16].
    • Pulkkinen L, Smith FJ, Shimizu H, Murata S, Yaoita H, Hachisuka H, Nishikawa T, McLean WH, Uitto J. Homozygous deletion mutations in the plectin gene (PLEC1) in patients with epidermolysis bullosa simplex associated with late-onset muscular dystrophy. of outstanding interest Hum Mol Genet. 5:1996;1539-1546 The demonstration that mutations in a cytoskeletal linker protein such as plectin can cause a human disease characterized by a lack of cell integrity was a clear indication of plectin's essential function in different cell types and argued strongly for the importance of other linker proteins. See also [13,14,16].
    • (1996) Hum Mol Genet , vol.5 , pp. 1539-1546
    • Pulkkinen, L.1    Smith, F.J.2    Shimizu, H.3    Murata, S.4    Yaoita, H.5    Hachisuka, H.6    Nishikawa, T.7    McLean, W.H.8    Uitto, J.9
  • 16
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • of outstanding interest. By disrupting the plectin gene in mice, these authors demonstrate the importance of the abundant cytoskeletal cross-linking protein plectin for reinforcement of several tissues. The defects displayed by these mice are most similar to the human disease muscular dystrophy with epidermolysis bullosa, which was also recently shown (in 14]) to result from a loss of plectin
    • Andra K, Lassmann H, Bittner R, Shorny S, Fassler R, Propst F, Wiche G. Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. of outstanding interest Genes Dev. 1997; By disrupting the plectin gene in mice, these authors demonstrate the importance of the abundant cytoskeletal cross-linking protein plectin for reinforcement of several tissues. The defects displayed by these mice are most similar to the human disease muscular dystrophy with epidermolysis bullosa, which was also recently shown (in 14]) to result from a loss of plectin.
    • (1997) Genes Dev
    • Andra, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fassler, R.5    Propst, F.6    Wiche, G.7
  • 17
    • 0029976981 scopus 로고    scopus 로고
    • Identification of a 450kDa autoantigen as a new member of the plectin family
    • Fujiwara S, Kohno K, Iwamatsu A, Naito I, Shinki H. Identification of a 450kDa autoantigen as a new member of the plectin family. J Invest Dermatol. 106:1996;1125-1130.
    • (1996) J Invest Dermatol , vol.106 , pp. 1125-1130
    • Fujiwara, S.1    Kohno, K.2    Iwamatsu, A.3    Naito, I.4    Shinki, H.5
  • 18
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo L, Degenstein L, Dowling J, Yu QC, Wollmann R, Perman B, Fuchs E. Gene targeting of BPAG1: abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell. 81:1995;233-243.
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 19
    • 0029035706 scopus 로고
    • The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1
    • Brown A, Bernier G, Mathieu M, Rossant J, Kothary R. The mouse dystonia musculorum gene is a neural isoform of bullous pemphigoid antigen 1. Nat Genet. 10:1995;301-306.
    • (1995) Nat Genet , vol.10 , pp. 301-306
    • Brown, A.1    Bernier, G.2    Mathieu, M.3    Rossant, J.4    Kothary, R.5
  • 20
    • 0030611639 scopus 로고    scopus 로고
    • Developmental expression of BPAG1-n: Insights into the spastic ataxia and gross neurologic degeneration in dystonia musculorum mice
    • of special interest. A more thorough examination of BPAG1n/dystonin expression in normal mice and the pathological changes caused by disrupting the BPAG locus in transgenic mice showed a less restricted expression pattern and distribution of neuronal abnormalities than was previously reported [18].
    • Dowling J, Yang Y, Wollmann R, Reichardt J, Fuchs E. Developmental expression of BPAG1-n: insights into the spastic ataxia and gross neurologic degeneration in dystonia musculorum mice. of special interest Dev Biol. 187:1997;131-142 A more thorough examination of BPAG1n/dystonin expression in normal mice and the pathological changes caused by disrupting the BPAG locus in transgenic mice showed a less restricted expression pattern and distribution of neuronal abnormalities than was previously reported [18].
    • (1997) Dev Biol , vol.187 , pp. 131-142
    • Dowling, J.1    Yang, Y.2    Wollmann, R.3    Reichardt, J.4    Fuchs, E.5
  • 21
    • 0029558104 scopus 로고
    • Dystonin expression in the developing nervous system predominates in the neurons that degenerate in dystonia musculorum mutant mice
    • Bernier G, Brown A, Dalpe G, de Repentigny Y, Mathieu M, Kothary R. Dystonin expression in the developing nervous system predominates in the neurons that degenerate in dystonia musculorum mutant mice. Mol Cell Neurosci. 6:1995;509-520.
    • (1995) Mol Cell Neurosci , vol.6 , pp. 509-520
    • Bernier, G.1    Brown, A.2    Dalpe, G.3    De Repentigny, Y.4    Mathieu, M.5    Kothary, R.6
  • 22
  • 23
    • 0025993428 scopus 로고
    • Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail
    • Yamasaki H, Itakura C, Mizutani M. Hereditary hypotrophic axonopathy with neurofilament deficiency in a mutant strain of the Japanese quail. Acta Neuropathol (Berl). 82:1991;427-434.
    • (1991) Acta Neuropathol (Berl) , vol.82 , pp. 427-434
    • Yamasaki, H.1    Itakura, C.2    Mizutani, M.3
  • 24
    • 0028261670 scopus 로고
    • Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-beta-galactosidase fusion protein
    • Eyer J, Peterson A. Neurofilament-deficient axons and perikaryal aggregates in viable transgenic mice expressing a neurofilament-beta-galactosidase fusion protein. Neuron. 12:1994;389-405.
    • (1994) Neuron , vol.12 , pp. 389-405
    • Eyer, J.1    Peterson, A.2
  • 25
    • 0031263931 scopus 로고    scopus 로고
    • Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments
    • of outstanding interest. Disruption of the neurofilament-L gene in mice resulted in the production of axons without neurofilaments, reduced axonal diameter, and axonal regeneration defects. These animals are another example supporting the view that filament number is a key determinant of axonal caliber
    • Zhu Q, Couillard-Despres S, Julien J-P. Delayed maturation of regenerating myelinated axons in mice lacking neurofilaments. of outstanding interest Exp Neurol. 1997; Disruption of the neurofilament-L gene in mice resulted in the production of axons without neurofilaments, reduced axonal diameter, and axonal regeneration defects. These animals are another example supporting the view that filament number is a key determinant of axonal caliber.
    • (1997) Exp Neurol
    • Zhu, Q.1    Couillard-Despres, S.2    Julien, J.-P.3
  • 26
    • 0029807823 scopus 로고    scopus 로고
    • Neurofilament subunit NF-H modulates axonal diameter by affecting the rate or neurofilament transport
    • of special interest. With a series of transgenic mice expressing completely wild-type mouse NF-H at up to four times the normal amount, this work demonstrates a selective slowing of NF transport, but the absence of any neuronal degeneration under these conditions. This indicates that that motor neuron disease developed by mice expressing human NF-H must arise from the human protein acting like a mutant in mice.
    • Marszalek JR, Williamson TL, Lee MK, Xu Z-S, Crawford TO, Hoffman PN, Cleveland DW. Neurofilament subunit NF-H modulates axonal diameter by affecting the rate or neurofilament transport. of special interest J Cell Biol. 135:1996;711-724 With a series of transgenic mice expressing completely wild-type mouse NF-H at up to four times the normal amount, this work demonstrates a selective slowing of NF transport, but the absence of any neuronal degeneration under these conditions. This indicates that that motor neuron disease developed by mice expressing human NF-H must arise from the human protein acting like a mutant in mice.
    • (1996) J Cell Biol , vol.135 , pp. 711-724
    • Marszalek, J.R.1    Williamson, T.L.2    Lee, M.K.3    Xu Z-S4    Crawford, T.O.5    Hoffman, P.N.6    Cleveland, D.W.7
  • 27
    • 0029894157 scopus 로고    scopus 로고
    • Subunit composition of neurofilaments specifies axonal diameter
    • of special interest. By mating transgenic mice expressing elevated levels of murine NF-L, NF-M or NF-H, to produce mice with elevated synthesis of any pair of subunits, this work demonstrates that NF-dependent stimulation of growth in axonal diameter requires NF-L to drive assembly and NF-M and NF-H to mediate interactions in the axoplasm.
    • Xu Z-S, Marszalek JR, Lee MK, Wong PC, Folmer J, Crawford TO, Hsieh S-T, Griffin JW, Cleveland DW. Subunit composition of neurofilaments specifies axonal diameter. of special interest J Cell Biol. 133:1996;1061-1069 By mating transgenic mice expressing elevated levels of murine NF-L, NF-M or NF-H, to produce mice with elevated synthesis of any pair of subunits, this work demonstrates that NF-dependent stimulation of growth in axonal diameter requires NF-L to drive assembly and NF-M and NF-H to mediate interactions in the axoplasm.
    • (1996) J Cell Biol , vol.133 , pp. 1061-1069
    • Xu Z-S1    Marszalek, J.R.2    Lee, M.K.3    Wong, P.C.4    Folmer, J.5    Crawford, T.O.6    Hsieh S-T7    Griffin, J.W.8    Cleveland, D.W.9
  • 28
    • 0029052277 scopus 로고
    • Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits
    • Tu PH, Elder G, Lazzarini RA, Nelson D, Trojanowski JQ, Lee VM. Overexpression of the human NFM subunit in transgenic mice modifies the level of endogenous NFL and the phosphorylation state of NFH subunits. J Cell Biol. 129:1995;1629-1640.
    • (1995) J Cell Biol , vol.129 , pp. 1629-1640
    • Tu, P.H.1    Elder, G.2    Lazzarini, R.A.3    Nelson, D.4    Trojanowski, J.Q.5    Lee, V.M.6
  • 29
    • 0029004898 scopus 로고
    • Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis
    • Collard JF, Cote F, Julien JP. Defective axonal transport in a transgenic mouse model of amyotrophic lateral sclerosis. Nature. 375:1995;61-64.
    • (1995) Nature , vol.375 , pp. 61-64
    • Collard, J.F.1    Cote, F.2    Julien, J.P.3
  • 30
    • 0027410516 scopus 로고
    • Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease
    • Xu Z, Cork LC, Griffin JW, Cleveland DW. Increased expression of neurofilament subunit NF-L produces morphological alterations that resemble the pathology of human motor neuron disease. Cell. 73:1993;23-33.
    • (1993) Cell , vol.73 , pp. 23-33
    • Xu, Z.1    Cork, L.C.2    Griffin, J.W.3    Cleveland, D.W.4
  • 31
    • 0027465098 scopus 로고
    • Progressive neuropathy in transgenic mice expressing the human neurofilament heavy gene: A mouse model of amyotrophic lateral sclerosis
    • Cote F, Collard JF, Julien JP. Progressive neuropathy in transgenic mice expressing the human neurofilament heavy gene: a mouse model of amyotrophic lateral sclerosis. Cell. 73:1993;35-46.
    • (1993) Cell , vol.73 , pp. 35-46
    • Cote, F.1    Collard, J.F.2    Julien, J.P.3
  • 32
    • 0028116467 scopus 로고
    • A mutant neurofilament subunit causes massive, selective motor neuron death: Implications for the pathogenesis of human motor neuron disease
    • Lee MK, Marszalek JR, Cleveland DW. A mutant neurofilament subunit causes massive, selective motor neuron death: implications for the pathogenesis of human motor neuron disease. Neuron. 13:1994;975-988.
    • (1994) Neuron , vol.13 , pp. 975-988
    • Lee, M.K.1    Marszalek, J.R.2    Cleveland, D.W.3
  • 33
    • 0029970685 scopus 로고    scopus 로고
    • Sequence variants in human neurofilament proteins: Absence of linkage to familial amyotrophic lateral sclerosis
    • Vechio JD, Bruijn LI, Xu Z, Brown RH Jr, Cleveland DW. Sequence variants in human neurofilament proteins: absence of linkage to familial amyotrophic lateral sclerosis. Ann Neurol. 40:1996;603-610.
    • (1996) Ann Neurol , vol.40 , pp. 603-610
    • Vechio, J.D.1    Bruijn, L.I.2    Xu, Z.3    Brown R.H., Jr.4    Cleveland, D.W.5
  • 34
    • 0030000608 scopus 로고    scopus 로고
    • Analysis of the KSP repeat of the neurofilament heavy subunit in familiar amyotrophic lateral sclerosis
    • Rooke K, Figlewicz DA, Han FY, Rouleau GA. Analysis of the KSP repeat of the neurofilament heavy subunit in familiar amyotrophic lateral sclerosis. Neurology. 46:1996;789-790.
    • (1996) Neurology , vol.46 , pp. 789-790
    • Rooke, K.1    Figlewicz, D.A.2    Han, F.Y.3    Rouleau, G.A.4
  • 35
    • 0028001606 scopus 로고
    • Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis
    • Figlewicz DA, Krizus A, Martinoli MG, Meininger V, Dib M, Rouleau GA, Julien J-P. Variants of the heavy neurofilament subunit are associated with the development of amyotrophic lateral sclerosis. Hum Mol Genet. 3:1994;1757-1761.
    • (1994) Hum Mol Genet , vol.3 , pp. 1757-1761
    • Figlewicz, D.A.1    Krizus, A.2    Martinoli, M.G.3    Meininger, V.4    Dib, M.5    Rouleau, G.A.6    Julien J-P7
  • 37
    • 0030034545 scopus 로고    scopus 로고
    • SOD1 mutation is associated with accumulation of neurofilaments in amyotrophic lateral sclerosis
    • of special interest. This work demonstrates that neurofilament misaccumulation, itself capable of causing motor neuron disease, is a downstream consequence of a mutation in superoxide dismutase 1 that causes amyotrophic lateral sclerosis.
    • Rouleau GA, Clark AW, Rooke K, Pramatarova A, Krizus A, Suchowersky O, Julien JP, Figlewicz D. SOD1 mutation is associated with accumulation of neurofilaments in amyotrophic lateral sclerosis. of special interest Ann Neurol. 39:1996;128-131 This work demonstrates that neurofilament misaccumulation, itself capable of causing motor neuron disease, is a downstream consequence of a mutation in superoxide dismutase 1 that causes amyotrophic lateral sclerosis.
    • (1996) Ann Neurol , vol.39 , pp. 128-131
    • Rouleau, G.A.1    Clark, A.W.2    Rooke, K.3    Pramatarova, A.4    Krizus, A.5    Suchowersky, O.6    Julien, J.P.7    Figlewicz, D.8
  • 38
    • 0029927679 scopus 로고    scopus 로고
    • Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement
    • Shibata N, Hirano A, Kobayashi M, Siddique T, Deng HX, Hung WY, Kato T, Asayama K. Intense superoxide dismutase-1 immunoreactivity in intracytoplasmic hyaline inclusions of familial amyotrophic lateral sclerosis with posterior column involvement. J Neuropathol Exp Neurol. 55:1996;481-490.
    • (1996) J Neuropathol Exp Neurol , vol.55 , pp. 481-490
    • Shibata, N.1    Hirano, A.2    Kobayashi, M.3    Siddique, T.4    Deng, H.X.5    Hung, W.Y.6    Kato, T.7    Asayama, K.8
  • 39
    • 0029738727 scopus 로고    scopus 로고
    • Disruption of muscle architecture and myocardial degeneration in mice lacking desmin
    • of outstanding interest. This work showed directly that desmin imparts the strength and structural integrity that are necessary for all three muscle types. A lack of desmin in mice does not preclude muscle formation, but does result in mitochondrial disorganization, myofiber misalignment, and degeneration.
    • Milner DJ, Weitzer G, Tran D, Bradley A, Capetanaki Y. Disruption of muscle architecture and myocardial degeneration in mice lacking desmin. of outstanding interest J Cell Biol. 134:1996;1255-1270 This work showed directly that desmin imparts the strength and structural integrity that are necessary for all three muscle types. A lack of desmin in mice does not preclude muscle formation, but does result in mitochondrial disorganization, myofiber misalignment, and degeneration.
    • (1996) J Cell Biol , vol.134 , pp. 1255-1270
    • Milner, D.J.1    Weitzer, G.2    Tran, D.3    Bradley, A.4    Capetanaki, Y.5
  • 40
    • 0029893923 scopus 로고    scopus 로고
    • Cardiovascular lesions and skeletal myopathy in mice lacking desmin
    • of special interest. of outstanding interest. Together with [39,41], this work with desmin-deficient mice demonstrates the importance of desmin in maintaining the structural integrity of highly used muscle types and proves that desmin is not necessary for the formation of muscle during development.
    • of special interest Li Z, Colucci-Guyon E, Pincon-Raymond M, Mericskay M, Pournin S, Paulin D, Babinet C. Cardiovascular lesions and skeletal myopathy in mice lacking desmin. of outstanding interest Dev Biol. 175:1996;362-366 Together with [39,41], this work with desmin-deficient mice demonstrates the importance of desmin in maintaining the structural integrity of highly used muscle types and proves that desmin is not necessary for the formation of muscle during development.
    • (1996) Dev Biol , vol.175 , pp. 362-366
    • Li, Z.1    Colucci-Guyon, E.2    Pincon-Raymond, M.3    Mericskay, M.4    Pournin, S.5    Paulin, D.6    Babinet, C.7
  • 41
    • 0030879081 scopus 로고    scopus 로고
    • Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle
    • of outstanding interest. of special interest. Together with [39,40], this work with desmin-deficient mice demonstrates the importance of desmin in maintaining the structural integrity of highly used muscle types and proves that desmin is not necessary for the formation of muscle during development.
    • of outstanding interest Li Z, Mericskay M, Agbulut O, Butler-Borwne G, Carlsson L, Thronell L-E, Babinet C, Paulin D. Desmin is essential for the tensile strength and integrity of myofibrils but not for myogenic commitment, differentiation, and fusion of skeletal muscle. of special interest J Cell Biol. 139:1997;1-16 Together with [39,40], this work with desmin-deficient mice demonstrates the importance of desmin in maintaining the structural integrity of highly used muscle types and proves that desmin is not necessary for the formation of muscle during development.
    • (1997) J Cell Biol , vol.139 , pp. 1-16
    • Li, Z.1    Mericskay, M.2    Agbulut, O.3    Butler-Borwne, G.4    Carlsson, L.5    Thronell L-E6    Babinet, C.7    Paulin, D.8
  • 42
    • 0026082642 scopus 로고
    • Suppression by antisense mRNA demonstrates a requirement for the glial fibrillary acidic protein in the formation of stable astrocytic processes in response to neurons
    • Weinstein DE, Shelanski ML, Liem RK. Suppression by antisense mRNA demonstrates a requirement for the glial fibrillary acidic protein in the formation of stable astrocytic processes in response to neurons. J Cell Biol. 112:1991;1205-1213.
    • (1991) J Cell Biol , vol.112 , pp. 1205-1213
    • Weinstein, D.E.1    Shelanski, M.L.2    Liem, R.K.3
  • 43
    • 0028878797 scopus 로고
    • Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions
    • Gomi H, Yokoyama T, Fujimoto K, Ikeda T, Katoh A, Itoh T, Itohara S. Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions. Neuron. 14:1995;29-41.
    • (1995) Neuron , vol.14 , pp. 29-41
    • Gomi, H.1    Yokoyama, T.2    Fujimoto, K.3    Ikeda, T.4    Katoh, A.5    Itoh, T.6    Itohara, S.7
  • 44
    • 0029012164 scopus 로고
    • Mice lacking glial fibrillary acidic protein display astrocytes devoid of intermediate filaments but develop and reproduce normally
    • Pekny M, Leveen P, Pekna M, Eliasson C, Berthold C-H, Westermark B, Betsholtz C. Mice lacking glial fibrillary acidic protein display astrocytes devoid of intermediate filaments but develop and reproduce normally. EMBO J. 14:1995;1590-1598.
    • (1995) EMBO J , vol.14 , pp. 1590-1598
    • Pekny, M.1    Leveen, P.2    Pekna, M.3    Eliasson, C.4    Berthold C-H5    Westermark, B.6    Betsholtz, C.7
  • 46
    • 0030273614 scopus 로고    scopus 로고
    • GFAP is necessary for the integrity of CNS white matter architecture and long-term maintenance of myelination
    • of special interest. More detailed examination of older mice lacking GFAP revealed defects in axon myelination and white matter abnormalities that were not apparent in earlier efforts [43,44]. With [47], it demonstrates the surprisingly subtle effects of removing the primary intermediate filament constituent, GFAP, from support cells of the CNS.
    • Liedtke W, Edelmann W, Bieri PL, Chiu F-C, Cowan NJ, Kucherlapati R, Raine CS. GFAP is necessary for the integrity of CNS white matter architecture and long-term maintenance of myelination. of special interest Neuron. 17:1996;607-615 More detailed examination of older mice lacking GFAP revealed defects in axon myelination and white matter abnormalities that were not apparent in earlier efforts [43,44]. With [47], it demonstrates the surprisingly subtle effects of removing the primary intermediate filament constituent, GFAP, from support cells of the CNS.
    • (1996) Neuron , vol.17 , pp. 607-615
    • Liedtke, W.1    Edelmann, W.2    Bieri, P.L.3    Chiu F-C4    Cowan, N.J.5    Kucherlapati, R.6    Raine, C.S.7
  • 47
    • 13344269673 scopus 로고    scopus 로고
    • Deficient cerebellar long term depression, impaired eyeblink conditioning, and normal motor coordination in glial fibrillary acidic protein mutant mice
    • of special interest. Mice devoid of glial fibrillary acidic protein were found to be deficient in a form of motor learning that is thought to be mediated by long-term depression, supporting the view that astrocytes can modulate higher neuronal functions.
    • Shibuki K, Gomi H, Chen L, Bao S, Kim JJ, Wakasuki H, Fujisaki T, Fujimoto K, Katoh A, Ikeda T, et al. Deficient cerebellar long term depression, impaired eyeblink conditioning, and normal motor coordination in glial fibrillary acidic protein mutant mice. of special interest Neuron. 16:1996;587-599 Mice devoid of glial fibrillary acidic protein were found to be deficient in a form of motor learning that is thought to be mediated by long-term depression, supporting the view that astrocytes can modulate higher neuronal functions.
    • (1996) Neuron , vol.16 , pp. 587-599
    • Shibuki, K.1    Gomi, H.2    Chen, L.3    Bao, S.4    Kim, J.J.5    Wakasuki, H.6    Fujisaki, T.7    Fujimoto, K.8    Katoh, A.9    Ikeda, T.10
  • 48
    • 0030014855 scopus 로고    scopus 로고
    • Disrupted glial fibrillary acidic protein network in astrocytes from vimentin knockout mice
    • of special interest. This report demonstrated that mature astrocytes normally co-expressing vimentin and glial fibrillary acidic protein (GFAP) require the presence of vimentin for normal assembly of a GFAP network, whereas other astrocytes that only expressed vimentin during development from GFAP structures in the absence of vimentin. This represents the first step in understanding the differential IF requirements of even highly related cell types.
    • Galou M, Colucci-Guyon E, Ensergueix D, Ridet JL, Gimenez Y, Ribotta M, Privat A, Babinet C, Dupouey P. Disrupted glial fibrillary acidic protein network in astrocytes from vimentin knockout mice. of special interest J Cell Biol. 133:1996;853-863 This report demonstrated that mature astrocytes normally co-expressing vimentin and glial fibrillary acidic protein (GFAP) require the presence of vimentin for normal assembly of a GFAP network, whereas other astrocytes that only expressed vimentin during development from GFAP structures in the absence of vimentin. This represents the first step in understanding the differential IF requirements of even highly related cell types.
    • (1996) J Cell Biol , vol.133 , pp. 853-863
    • Galou, M.1    Colucci-Guyon, E.2    Ensergueix, D.3    Ridet, J.L.4    Gimenez, Y.5    Ribotta, M.6    Privat, A.7    Babinet, C.8    Dupouey, P.9
  • 50
    • 0029198668 scopus 로고
    • The dynamic properties and possible functions of nuclear lamins
    • Moir RD, Spann TP, Goldmann RD. The dynamic properties and possible functions of nuclear lamins. Int Rev Cytol. 162B:1995;141-181.
    • (1995) Int Rev Cytol , vol.162 , pp. 141-181
    • Moir, R.D.1    Spann, T.P.2    Goldmann, R.D.3
  • 51
    • 0030863126 scopus 로고    scopus 로고
    • Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis
    • of special interest. Use of dominant-negative mutant lamin proteins to disrupt nuclear lamin networks provides evidence for the ability of lamins to modulate nuclear processes such as DNA replication and nuclear reassembly.
    • Spann TP, Moir RD, Goldman AE, Stick R, Goldman RD. Disruption of nuclear lamin organization alters the distribution of replication factors and inhibits DNA synthesis. of special interest J Cell Biol. 136:1997;1201-1212 Use of dominant-negative mutant lamin proteins to disrupt nuclear lamin networks provides evidence for the ability of lamins to modulate nuclear processes such as DNA replication and nuclear reassembly.
    • (1997) J Cell Biol , vol.136 , pp. 1201-1212
    • Spann, T.P.1    Moir, R.D.2    Goldman, A.E.3    Stick, R.4    Goldman, R.D.5
  • 52
    • 0030575334 scopus 로고    scopus 로고
    • Keratin biochemistry
    • Albers KM. Keratin biochemistry. Clin Dermatol. 14:1996;309-320.
    • (1996) Clin Dermatol , vol.14 , pp. 309-320
    • Albers, K.M.1
  • 53
    • 0029810901 scopus 로고    scopus 로고
    • The genetic basis of epidermolysis bullosa simplex with mottled pigmentation
    • of special interest. This report is the first to identify a genetic mutation responsible for a rare subtype of epiermolysis bullosa simplex (EBS), EBS with mottled pigmentation. Also of note, this mutation occurs within the head domain of keratin 5, whereas most other disease-causing keratin mutations have been shown to reside in the more conserved ends of the rod domain.
    • Uttam J, Hutton E, Coulombe PA, Anton-Lamprecht I, Yu QC, Gedde-Dahl T Jr, Fine JD, Fuschs E. The genetic basis of epidermolysis bullosa simplex with mottled pigmentation. of special interest Proc Natl Acad Sci USA. 93:1996;9079-9084 This report is the first to identify a genetic mutation responsible for a rare subtype of epiermolysis bullosa simplex (EBS), EBS with mottled pigmentation. Also of note, this mutation occurs within the head domain of keratin 5, whereas most other disease-causing keratin mutations have been shown to reside in the more conserved ends of the rod domain.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 9079-9084
    • Uttam, J.1    Hutton, E.2    Coulombe, P.A.3    Anton-Lamprecht, I.4    Yu, Q.C.5    Gedde-Dahl T., Jr.6    Fine, J.D.7    Fuschs, E.8
  • 55
    • 0030474645 scopus 로고    scopus 로고
    • The cytoskeleton and disease: Genetic disorders of intermediate filaments
    • Fuchs E. The cytoskeleton and disease: genetic disorders of intermediate filaments. Annu Rev Genet. 30:1996;197-231.
    • (1996) Annu Rev Genet , vol.30 , pp. 197-231
    • Fuchs, E.1
  • 56
    • 0031029525 scopus 로고    scopus 로고
    • Mutation of human keratin 18 in association with cryptogenic cirrhosis
    • of special interest. These investigators show for the first time that a mutation within the keratin pair K8/K18 may account for human liver disease of unknown etiology, in accordance with previous work using K8-null mice which die during embryo-genesis as a result of liver hemorrhage.
    • Ku NO, Wright TL, Terrault NA, Gish R, Omary MB. Mutation of human keratin 18 in association with cryptogenic cirrhosis. of special interest J Clin Invest. 99:1997;19-23 These investigators show for the first time that a mutation within the keratin pair K8/K18 may account for human liver disease of unknown etiology, in accordance with previous work using K8-null mice which die during embryo-genesis as a result of liver hemorrhage.
    • (1997) J Clin Invest , vol.99 , pp. 19-23
    • Ku, N.O.1    Wright, T.L.2    Terrault, N.A.3    Gish, R.4    Omary, M.B.5
  • 58
    • 0030747138 scopus 로고    scopus 로고
    • Mutations in the hair cortex keratin hHb6 cause the inherited hair disease monilethrix
    • of special interest. This first description of a mutation in a hard α-keratin that causes an inherited hair disease demonstrates the universal requirement for keratins in the varied cell types they inhabit.
    • Winter H, Rogers MA, Langbein L, Stevens HP, Leigh IM, Labreze C, Roul S, Taieb A, Kreit T, Schweizer J. Mutations in the hair cortex keratin hHb6 cause the inherited hair disease monilethrix. of special interest Nat Genet. 16:1997;372-374 This first description of a mutation in a hard α-keratin that causes an inherited hair disease demonstrates the universal requirement for keratins in the varied cell types they inhabit.
    • (1997) Nat Genet , vol.16 , pp. 372-374
    • Winter, H.1    Rogers, M.A.2    Langbein, L.3    Stevens, H.P.4    Leigh, I.M.5    Labreze, C.6    Roul, S.7    Taieb, A.8    Kreit, T.9    Schweizer, J.10
  • 59
    • 0029905020 scopus 로고    scopus 로고
    • A transgenic mouse model with an inducible skin blistering disease phenotype
    • of outstanding interest. This work used the keratin 6 promoter inducibly to express a heterologous gene product in the skin of mice. The utility of the system was demonstrated by producing mice that developed a skin blistering disease most similar to IBS (icthyosis bullosa of Siemens) upon induction of a keratin 6a mutation. The work sets the stage for delivery of foreign gene products via transgenic skin grafts. See also [60].
    • Takahashi K, Coulombe PA. A transgenic mouse model with an inducible skin blistering disease phenotype. of outstanding interest Proc Natl Acad Sci USA. 93:1996;14776-14781 This work used the keratin 6 promoter inducibly to express a heterologous gene product in the skin of mice. The utility of the system was demonstrated by producing mice that developed a skin blistering disease most similar to IBS (icthyosis bullosa of Siemens) upon induction of a keratin 6a mutation. The work sets the stage for delivery of foreign gene products via transgenic skin grafts. See also [60].
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14776-14781
    • Takahashi, K.1    Coulombe, P.A.2
  • 60
    • 0031031056 scopus 로고    scopus 로고
    • Transgenic studies with a keratin promoter-driven growth hormone transgene: Prospects for gene therapy
    • of outstanding interest. The keratin 14 promoter was used to drive expression of a growth hormone in the skin of mice. Skin grafts from such donor mice could be transferred to recipient mice to sustain increased levels of the hormone in the blood stream, demonstrating the possible utility of this system for human gene therapy by delivering products secreted by grafted skin cells. See also [59].
    • Wang X, Zinkel S, Polonsky K, Fuchs E. Transgenic studies with a keratin promoter-driven growth hormone transgene: prospects for gene therapy. of outstanding interest Proc Natl Acad Sci USA. 94:1997;219-226 The keratin 14 promoter was used to drive expression of a growth hormone in the skin of mice. Skin grafts from such donor mice could be transferred to recipient mice to sustain increased levels of the hormone in the blood stream, demonstrating the possible utility of this system for human gene therapy by delivering products secreted by grafted skin cells. See also [59].
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 219-226
    • Wang, X.1    Zinkel, S.2    Polonsky, K.3    Fuchs, E.4


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