메뉴 건너뛰기




Volumn 10, Issue 1, 2000, Pages 17-24

The kelch repeat superfamily of proteins: Propellers of cell function

Author keywords

[No Author keywords available]

Indexed keywords

CELL FUNCTION; CYTOSKELETON; DROSOPHILA; EVOLUTION; EXTRACELLULAR MATRIX; OPEN READING FRAME; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE; REVIEW; TANDEM REPEAT;

EID: 0033961690     PISSN: 09628924     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0962-8924(99)01673-6     Document Type: Review
Times cited : (526)

References (53)
  • 1
    • 0027403024 scopus 로고
    • Kelch encodes a component of intercellular bridges in Drosophila egg chambers
    • 1 Xue, F. and Cooley, L. (1993) kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 72, 681-693
    • (1993) Cell , vol.72 , pp. 681-693
    • Xue, F.1    Cooley, L.2
  • 2
    • 0028231273 scopus 로고
    • Drosophila kelch motif is derived from a common enzyme fold
    • 2 Bork, P. and Doolittle, R.F. (1994) Drosophila kelch motif is derived from a common enzyme fold. J. Mol. Biol. 236, 1277-1282
    • (1994) J. Mol. Biol. , vol.236 , pp. 1277-1282
    • Bork, P.1    Doolittle, R.F.2
  • 3
    • 0033574503 scopus 로고    scopus 로고
    • Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches
    • 3 Aravind, L. and Koonin, E.V. (1999) Gleaning non-trivial structural, functional and evolutionary information about proteins by iterative database searches. J. Mol. Biol. 287, 1023-1040
    • (1999) J. Mol. Biol. , vol.287 , pp. 1023-1040
    • Aravind, L.1    Koonin, E.V.2
  • 4
    • 0028290823 scopus 로고
    • Crystal structure of a free radical enzyme, galactose oxidase
    • 4 Ito, N. et al. (1994) Crystal structure of a free radical enzyme, galactose oxidase. J. Mol. Biol. 238, 794-814
    • (1994) J. Mol. Biol. , vol.238 , pp. 794-814
    • Ito, N.1
  • 5
    • 0029593456 scopus 로고
    • The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2
    • 5 Wall, M.A. et al. (1995) The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Cell 83, 1047-1058
    • (1995) Cell , vol.83 , pp. 1047-1058
    • Wall, M.A.1
  • 6
    • 0029664589 scopus 로고    scopus 로고
    • The 2 Å crystal structure of a heterotrimeric G protein
    • 6 Lambright, D.G. et al. (1996) The 2 Å crystal structure of a heterotrimeric G protein. Nature 379, 311-319
    • (1996) Nature , vol.379 , pp. 311-319
    • Lambright, D.G.1
  • 7
    • 0032485075 scopus 로고    scopus 로고
    • The 1 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller
    • 7 Renault, L. (1998) The 1 Å crystal structure of the regulator of chromosome condensation (RCC1) reveals a seven-bladed propeller. Nature 392, 97-101
    • (1998) Nature , vol.392 , pp. 97-101
    • Renault, L.1
  • 8
    • 0032514995 scopus 로고    scopus 로고
    • Atomic structure of clathrin: A beta propeller terminal domain joins an alpha zigzag linker
    • 8 ter Haar, E. et al. (1998) Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. Cell 95, 563-573
    • (1998) Cell , vol.95 , pp. 563-573
    • Ter Haar, E.1
  • 9
    • 0033133919 scopus 로고    scopus 로고
    • The WD repeat: A common architecture for diverse functions
    • 9 Smith, T.F. et al. (1999) The WD repeat: a common architecture for diverse functions. Trends Biochem. Sci. 24, 181-185
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 181-185
    • Smith, T.F.1
  • 10
    • 0026671355 scopus 로고
    • Structural principles for the propeller assembly of beta-sheets: The preference for seven-fold symmetry
    • 10 Murzin, A.G. (1992) Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry. Proteins 14, 191-201
    • (1992) Proteins , vol.14 , pp. 191-201
    • Murzin, A.G.1
  • 11
    • 0028915336 scopus 로고
    • Isolation and characterization of a novel gene deleted in DiGeorge syndrome
    • 11 Kurahashi, H. et al. (1995) Isolation and characterization of a novel gene deleted in DiGeorge syndrome. Hum. Mol. Genet. 4, 541-549
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 541-549
    • Kurahashi, H.1
  • 12
    • 0031745007 scopus 로고    scopus 로고
    • DNA sequence and muscle-specific expression of human sarcosin transcripts
    • 12 Taylor, A. et al. (1998) DNA sequence and muscle-specific expression of human sarcosin transcripts. Mol. Cell. Biochem. 183, 105-112
    • (1998) Mol. Cell. Biochem. , vol.183 , pp. 105-112
    • Taylor, A.1
  • 13
    • 0025183685 scopus 로고
    • The complete DNA sequence of Vaccinia virus
    • 13 Goebel, S.J. et al. (1990) The complete DNA sequence of Vaccinia virus. Virology 179, 247-266
    • (1990) Virology , vol.179 , pp. 247-266
    • Goebel, S.J.1
  • 14
    • 0033019824 scopus 로고    scopus 로고
    • Myxoma virus encodes an alpha2, 3-sialyltransferase that enhances virulence
    • 14 Jackson, R.J. et al. (1999) Myxoma virus encodes an alpha2, 3-sialyltransferase that enhances virulence. J. Virol. 73, 2376-2384
    • (1999) J. Virol. , vol.73 , pp. 2376-2384
    • Jackson, R.J.1
  • 15
    • 0029949657 scopus 로고    scopus 로고
    • A novel type of protein kinase phosphorylates actin in the actin-fragmin complex
    • 15 Eichinger, L. et al. (1996) A novel type of protein kinase phosphorylates actin in the actin-fragmin complex. EMBO J. 15, 5547-5556
    • (1996) EMBO J. , vol.15 , pp. 5547-5556
    • Eichinger, L.1
  • 16
    • 0028851246 scopus 로고
    • Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm
    • 16 Way, M. et al. (1995) Sequence and domain organization of scruin, an actin-cross-linking protein in the acrosomal process of Limulus sperm. J. Cell Biol. 128, 51-60
    • (1995) J. Cell Biol. , vol.128 , pp. 51-60
    • Way, M.1
  • 17
    • 0028115630 scopus 로고
    • Three-dimensional structrue of a single filament in the Limulus acrosomal bundle: Scruin binds to homologous helix-loop-beta motifs in actin
    • 17 Schmid, M.F. et al. (1994) Three-dimensional structrue of a single filament in the Limulus acrosomal bundle: scruin binds to homologous helix-loop-beta motifs in actin. J. Cell Biol. 124, 341-350
    • (1994) J. Cell Biol. , vol.124 , pp. 341-350
    • Schmid, M.F.1
  • 18
    • 0030989488 scopus 로고    scopus 로고
    • ENC-1: A novel mammalian Kelch-related gene specifically expressed in the nervous system encodes an actin-binding protein
    • 18 Hernandez, M.C. et al. (1997) ENC-1: a novel mammalian Kelch-related gene specifically expressed in the nervous system encodes an actin-binding protein. J. Neurosci. 17, 3038-3051
    • (1997) J. Neurosci. , vol.17 , pp. 3038-3051
    • Hernandez, M.C.1
  • 19
    • 0032146921 scopus 로고    scopus 로고
    • Cloning of human ENC-1 and evaluation of its expression and regulation in nervous system tumors
    • 19 Hernandez, M.C. et al. (1998) Cloning of human ENC-1 and evaluation of its expression and regulation in nervous system tumors. Exp. Cell Res. 242, 470-477
    • (1998) Exp. Cell Res. , vol.242 , pp. 470-477
    • Hernandez, M.C.1
  • 20
    • 0033522185 scopus 로고    scopus 로고
    • Isolation and characterization of IPP, a novel human gene encoding an actin-binding, kelch-like protein
    • 20 Kim, I.F. et al. (1999) Isolation and characterization of IPP, a novel human gene encoding an actin-binding, kelch-like protein. Gene 228, 73-83
    • (1999) Gene , vol.228 , pp. 73-83
    • Kim, I.F.1
  • 21
    • 0030757226 scopus 로고    scopus 로고
    • Drosophila kelch is an oligomeric ring canal actin organizer
    • 21 Robinson, D.N. and Cooley, L. (1997) Drosophila kelch is an oligomeric ring canal actin organizer. J. Cell Biol. 138, 799-810
    • (1997) J. Cell Biol. , vol.138 , pp. 799-810
    • Robinson, D.N.1    Cooley, L.2
  • 22
    • 0032816182 scopus 로고    scopus 로고
    • Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain
    • 22 Soltysik-Espanola, M. et al. (1999) Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain. Mol. Biol. Cell 10, 2361-2375
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2361-2375
    • Soltysik-Espanola, M.1
  • 23
    • 0028980644 scopus 로고
    • Beta-scruin, a homologue of the actin cross-linking protein scruin, is localised to the acrosomal vesicle of Limulus sperm
    • 23 Way, M. et al. (1995) Beta-scruin, a homologue of the actin cross-linking protein scruin, is localised to the acrosomal vesicle of Limulus sperm. J. Cell Sci. 108, 3155-3162
    • (1995) J. Cell Sci. , vol.108 , pp. 3155-3162
    • Way, M.1
  • 24
    • 0029148609 scopus 로고
    • Molecular nature of calicin, a major basic protein of the mammalian sperm head cytoskeleton
    • 24 von Bulow, M. et al. (1995) Molecular nature of calicin, a major basic protein of the mammalian sperm head cytoskeleton. Exp. Cell Res. 219, 407-413
    • (1995) Exp. Cell Res. , vol.219 , pp. 407-413
    • Von Bulow, M.1
  • 25
    • 0032547791 scopus 로고    scopus 로고
    • Identification of Kel1p, a kelch domain-containing protein involved in cell fusion and morphology in Saccharomyces cerevisiae
    • 25 Philips, J. and Herskowitz, I. (1998) Identification of Kel1p, a kelch domain-containing protein involved in cell fusion and morphology in Saccharomyces cerevisiae. J. Cell Biol. 143, 375-389
    • (1998) J. Cell Biol. , vol.143 , pp. 375-389
    • Philips, J.1    Herskowitz, I.2
  • 26
    • 0032168509 scopus 로고    scopus 로고
    • Muskelin, a novel intracellular mediator of cell adhesive and cytoskeletal responses to thrombospondin-1
    • 26 Adams J.C. et al. (1998) Muskelin, a novel intracellular mediator of cell adhesive and cytoskeletal responses to thrombospondin-1. EMBO J. 17, 4964-4974
    • (1998) EMBO J. , vol.17 , pp. 4964-4974
    • Adams, J.C.1
  • 27
    • 0040973364 scopus 로고    scopus 로고
    • A novel Rab9 effector required for endosome to TGN transport
    • 27 Diaz, E. et al. (1997) A novel Rab9 effector required for endosome to TGN transport. J. Cell Biol. 138, 283-290
    • (1997) J. Cell Biol. , vol.138 , pp. 283-290
    • Diaz, E.1
  • 28
    • 0024408669 scopus 로고
    • Characterization of the Schizosaccharomyces pombe ral2 gene implicated in activation of the ras1 gene product
    • 28 Fukui, Y. et al. (1989) Characterization of the Schizosaccharomyces pombe ral2 gene implicated in activation of the ras1 gene product. Mol. Cell. Biol. 9, 5617-5622
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 5617-5622
    • Fukui, Y.1
  • 29
    • 0030773728 scopus 로고    scopus 로고
    • Tea1 and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell
    • 29 Mata, J. and Nurse, P. (1997) tea1 and the microtubular cytoskeleton are important for generating global spatial order within the fission yeast cell. Cell 89, 939-949
    • (1997) Cell , vol.89 , pp. 939-949
    • Mata, J.1    Nurse, P.2
  • 30
    • 0029042690 scopus 로고
    • The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to the actin-associated proteins kelch and scruin
    • 30 Varkey, J.P. et al. (1995) The Caenorhabditis elegans spe-26 gene is necessary to form spermatids and encodes a protein similar to the actin-associated proteins kelch and scruin. Genes Dev. 9, 1074-1086
    • (1995) Genes Dev. , vol.9 , pp. 1074-1086
    • Varkey, J.P.1
  • 31
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • 31 Itoh, K. et al. (1999) Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13, 76-86
    • (1999) Genes Dev. , vol.13 , pp. 76-86
    • Itoh, K.1
  • 32
    • 0032482230 scopus 로고    scopus 로고
    • NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation
    • 32 Kim, T.A. et al. (1998) NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation. J. Cell Biol. 141, 553-566
    • (1998) J. Cell Biol. , vol.141 , pp. 553-566
    • Kim, T.A.1
  • 33
    • 0025301095 scopus 로고
    • RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination
    • 33 Oettinger, M.A. et al. (1990) RAG-1 and RAG-2, adjacent genes that synergistically activate V(D)J recombination. Science 248, 1517-1523
    • (1990) Science , vol.248 , pp. 1517-1523
    • Oettinger, M.A.1
  • 34
    • 0030863636 scopus 로고    scopus 로고
    • VP16 targets an amino-terminal domain of HCF involved in cell cycle progression
    • 34 Wilson, A.C. et al. (1997) VP16 targets an amino-terminal domain of HCF involved in cell cycle progression. Mol. Cell. Biol. 17, 6139-6146
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 6139-6146
    • Wilson, A.C.1
  • 35
    • 0032897973 scopus 로고    scopus 로고
    • Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2
    • 35 Johnson, K.M. et al. (1999) Herpes simplex virus transactivator VP16 discriminates between HCF-1 and a novel family member, HCF-2. J. Virol. 73, 3930-3940
    • (1999) J. Virol. , vol.73 , pp. 3930-3940
    • Johnson, K.M.1
  • 36
    • 0031847217 scopus 로고    scopus 로고
    • NS1-binding protein (NS1-BP): A novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells
    • 36 Wolff, T. et al. (1998) NS1-binding protein (NS1-BP): a novel human protein that interacts with the influenza A virus nonstructural NS1 protein is relocalized in the nuclei of infected cells. J. Virol. 72, 7170-7180
    • (1998) J. Virol. , vol.72 , pp. 7170-7180
    • Wolff, T.1
  • 37
    • 0032530558 scopus 로고    scopus 로고
    • Attractin (DPPT-L), a member of the CUB family of cell adhesion and guidance proteins, is secreted by activated human T lymphocytes and modulates immune cell interactions
    • 37 Duke-Cohan, J.S. et al. (1998) Attractin (DPPT-L), a member of the CUB family of cell adhesion and guidance proteins, is secreted by activated human T lymphocytes and modulates immune cell interactions. Proc. Natl. Acad. Sci. U. S. A. 95, 11336-11341
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 11336-11341
    • Duke-Cohan, J.S.1
  • 38
    • 0026779232 scopus 로고
    • Galactose oxidase of Dactylium dendroide. Gene cloning and sequence analysis
    • 38 McPherson, M.J. et al. (1992) Galactose oxidase of Dactylium dendroide. Gene cloning and sequence analysis. J. Biol. Chem. 267, 8146-8152
    • (1992) J. Biol. Chem. , vol.267 , pp. 8146-8152
    • McPherson, M.J.1
  • 39
    • 0032812915 scopus 로고    scopus 로고
    • Kel-1, a novel Kelch-related gene in Caenorhabditis elegans, is expressed in pharyngeal gland cells and is required for the feeding process
    • 39 Ohmachi, M. et al. (1999) kel-1, a novel Kelch-related gene in Caenorhabditis elegans, is expressed in pharyngeal gland cells and is required for the feeding process. Genes Cells 4, 325-337
    • (1999) Genes Cells , vol.4 , pp. 325-337
    • Ohmachi, M.1
  • 40
    • 0033545681 scopus 로고    scopus 로고
    • The mouse mahogany locus encodes a transmembrane form of human attractin
    • 40 Gunn, T.M. et al. (1999) The mouse mahogany locus encodes a transmembrane form of human attractin. Nature 398, 152-156
    • (1999) Nature , vol.398 , pp. 152-156
    • Gunn, T.M.1
  • 41
    • 0033545572 scopus 로고    scopus 로고
    • The mahogany protein is a receptor involved in suppression of obesity
    • 41 Nagle, D.L. et al. (1999) The mahogany protein is a receptor involved in suppression of obesity. Nature 398, 148-152
    • (1999) Nature , vol.398 , pp. 148-152
    • Nagle, D.L.1
  • 42
    • 0030059923 scopus 로고    scopus 로고
    • Characterization of the actin cross-linking properties of the scruin-calmodulin complex from the acrosomal process of Limulus sperm
    • 42 Sanders, M.C. et al. (1996) Characterization of the actin cross-linking properties of the scruin -calmodulin complex from the acrosomal process of Limulus sperm. J. Biol. Chem. 271, 2651-2657
    • (1996) J. Biol. Chem. , vol.271 , pp. 2651-2657
    • Sanders, M.C.1
  • 43
    • 0026026477 scopus 로고
    • Presence and localization of the 60 kD calicin in human spermatozoa presenting postacrosomal sheath defects: Preliminary results
    • 43 Courtot, A-M. (1991) Presence and localization of the 60 kD calicin in human spermatozoa presenting postacrosomal sheath defects: preliminary results. Mol. Reprod. Dev. 28, 272-279
    • (1991) Mol. Reprod. Dev. , vol.28 , pp. 272-279
    • Courtot, A.-M.1
  • 44
    • 0031826699 scopus 로고    scopus 로고
    • Distinct roles of RAG1 and RAG2 in binding the V(D)J recombination signal sequences
    • 44 Akamatsu, Y. and Oettinger, M.A. (1998) Distinct roles of RAG1 and RAG2 in binding the V(D)J recombination signal sequences. Mol. Cell. Biol. 18, 4670-4678
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4670-4678
    • Akamatsu, Y.1    Oettinger, M.A.2
  • 45
    • 0033548653 scopus 로고    scopus 로고
    • RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro
    • 45 Mo, X. et al. (1999) RAG1 and RAG2 cooperate in specific binding to the recombination signal sequence in vitro. J. Biol. Chem. 274, 7025-7031
    • (1999) J. Biol. Chem. , vol.274 , pp. 7025-7031
    • Mo, X.1
  • 46
    • 0031712128 scopus 로고    scopus 로고
    • The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis
    • 46 Callebaut, I. and Mornon, J-P. (1998) The V(D)J recombination activating protein RAG2 consists of a six-bladed propeller and a PHD fingerlike domain, as revealed by sequence analysis. Cell. Mol. Life Sci. 54, 880-891
    • (1998) Cell. Mol. Life Sci. , vol.54 , pp. 880-891
    • Callebaut, I.1    Mornon, J.-P.2
  • 47
    • 0040294788 scopus 로고    scopus 로고
    • Analysis of functional domains of the host cell factor involved in VP16 complex formation
    • 47 Hughes, T.A. et al. (1999) Analysis of functional domains of the host cell factor involved in VP16 complex formation. J. Biol. Chem. 274, 16437-16443
    • (1999) J. Biol. Chem. , vol.274 , pp. 16437-16443
    • Hughes, T.A.1
  • 48
    • 0031000133 scopus 로고    scopus 로고
    • Modification of Cys-837 identifies an actin-binding site in the beta-propeller protein scruin
    • 48 Sun, S. et al. (1997) Modification of Cys-837 identifies an actin-binding site in the beta-propeller protein scruin. Mol. Biol. Cell 8, 421-430
    • (1997) Mol. Biol. Cell , vol.8 , pp. 421-430
    • Sun, S.1
  • 49
    • 10144253125 scopus 로고    scopus 로고
    • RAG mutations in human B cell-negative SCID
    • 49 Schwarz, K. et al. (1996) RAG mutations in human B cell-negative SCID. Science 274, 97-99
    • (1996) Science , vol.274 , pp. 97-99
    • Schwarz, K.1
  • 50
    • 0032577548 scopus 로고    scopus 로고
    • Partial V(D)J recombination activity leads to Omenn syndrome
    • 50 Villa, A. et al. (1998) Partial V(D)J recombination activity leads to Omenn syndrome. Cell 93, 885-896
    • (1998) Cell , vol.93 , pp. 885-896
    • Villa, A.1
  • 51
    • 0344563603 scopus 로고    scopus 로고
    • Domain organization of Mac-2 binding and its oligomerisation to linear and ring-like structures
    • 51 Muller, S.A. et al. (1999) Domain organization of Mac-2 binding and its oligomerisation to linear and ring-like structures. J. Mol. Biol. 291, 801-813
    • (1999) J. Mol. Biol. , vol.291 , pp. 801-813
    • Muller, S.A.1
  • 52
    • 0032514737 scopus 로고    scopus 로고
    • Crystal structure of the BTB domain from PLZF
    • 52 Ahmad, K.F. et al. (1998) Crystal structure of the BTB domain from PLZF. Proc. Natl. Acad. Sci. U. S. A. 95, 12123-12128
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12123-12128
    • Ahmad, K.F.1
  • 53
    • 0033038381 scopus 로고    scopus 로고
    • Genomic structure and comparative analysis of nine Fugu genes: Conservation of synteny with human chromosome Xp22.2-p22.1
    • 53 Brunner, B. et al. (1999) Genomic structure and comparative analysis of nine Fugu genes: conservation of synteny with human chromosome Xp22.2-p22.1. Genome Res. 9, 437-448
    • (1999) Genome Res. , vol.9 , pp. 437-448
    • Brunner, B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.