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Volumn 19, Issue 3, 1999, Pages 2425-2434

The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; GROWTH FACTOR RECEPTOR KINASE; GUANOSINE TRIPHOSPHATASE; INTEGRIN; INTEGRIN LINKED KINASE; PROTEIN PINCH; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 0033020670     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.3.2425     Document Type: Article
Times cited : (250)

References (34)
  • 1
    • 0027203057 scopus 로고
    • The alpha v beta 3 integrin associates with a 190-kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor
    • Bartfeld, N. S., E. B. Pasquale, J. E. Geltosky, and L. R. Languino. 1993. The alpha v beta 3 integrin associates with a 190-kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor. J. Biol. Chem. 268:177270-17276.
    • (1993) J. Biol. Chem. , vol.268 , pp. 177270-217276
    • Bartfeld, N.S.1    Pasquale, E.B.2    Geltosky, J.E.3    Languino, L.R.4
  • 2
    • 0027333330 scopus 로고
    • Hundreds of ankyrin-like repeats in functionally diverse proteins: Mobile modules that cross phyla horizontally?
    • Bork, P. 1993. Hundreds of ankyrin-like repeats in functionally diverse proteins: mobile modules that cross phyla horizontally? Proteins 17:363-374.
    • (1993) Proteins , vol.17 , pp. 363-374
    • Bork, P.1
  • 3
    • 85038202794 scopus 로고    scopus 로고
    • Clontech Laboratories, Palo Alto, Calif.
    • Clontech. Yeast protocol handbook. Clontech Laboratories, Palo Alto, Calif.
    • Yeast Protocol Handbook
  • 4
    • 0026075528 scopus 로고
    • Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions
    • Crawford, A. W., and M. C. Beckerle. 1991. Purification and characterization of zyxin, an 82,000-dalton component of adherens junctions. J. Biol. Chem. 266:5847-5853.
    • (1991) J. Biol. Chem. , vol.266 , pp. 5847-5853
    • Crawford, A.W.1    Beckerle, M.C.2
  • 5
    • 0026586856 scopus 로고
    • An interaction between zyxin and alpha-actinin
    • Crawford, A. W., J. W. Michelsen, and M. C. Beckerle. 1992. An interaction between zyxin and alpha-actinin. J. Cell Biol. 116:1381-1393.
    • (1992) J. Cell Biol. , vol.116 , pp. 1381-1393
    • Crawford, A.W.1    Michelsen, J.W.2    Beckerle, M.C.3
  • 6
    • 0028158138 scopus 로고
    • Biochemical and molecular characterization of the chicken cysteine-rich protein, a developmentally regulated LIM-domain protein that is associated with the actin cytoskeleton
    • Crawford, A. W., J. D. Pino, and M. C. Beckerle. 1994. Biochemical and molecular characterization of the chicken cysteine-rich protein, a developmentally regulated LIM-domain protein that is associated with the actin cytoskeleton. J. Cell Biol. 124:117-127.
    • (1994) J. Cell Biol. , vol.124 , pp. 117-127
    • Crawford, A.W.1    Pino, J.D.2    Beckerle, M.C.3
  • 7
    • 0031966041 scopus 로고    scopus 로고
    • LIM domains: Multiple roles as adapters and functional modifiers in protein interactions
    • Dawid, I. B., J. J. Breen, and R. Toyama. 1998. LIM domains: multiple roles as adapters and functional modifiers in protein interactions. Trends Genet. 14:156-162.
    • (1998) Trends Genet. , vol.14 , pp. 156-162
    • Dawid, I.B.1    Breen, J.J.2    Toyama, R.3
  • 8
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signal transduction
    • Dedhar, S., and G. E. Hannigan. 1996. Integrin cytoplasmic interactions and bidirectional transmembrane signal transduction. Curr. Opin. Cell Biol. 8: 657-669.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 9
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne, M., C. Tan, V. Gray, L. Rue, J. Woodgett, and S. Dedhar. 1998. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. USA 95:11211-11216.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1    Tan, C.2    Gray, V.3    Rue, L.4    Woodgett, J.5    Dedhar, S.6
  • 10
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., A. St. Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 12
    • 85038199687 scopus 로고    scopus 로고
    • A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in C. elegans
    • in press
    • Hobert, O., D. G. Moerman, K. A. Clark, M. C. Beckerle., and G. Ruvkun. A conserved LIM protein that affects muscular adherens junction integrity and mechanosensory function in C. elegans. J. Cell Biol., in press.
    • J. Cell Biol.
    • Hobert, O.1    Moerman, D.G.2    Clark, K.A.3    Beckerle, M.C.4    Ruvkun, G.5
  • 14
    • 0030786162 scopus 로고    scopus 로고
    • Identification and characterization of a mouse protein kinase that is highly homologous to human integrin-linked kinase
    • Li, F., J. Liu, R. Mayne, and C. Wu. 1997. Identification and characterization of a mouse protein kinase that is highly homologous to human integrin-linked kinase. Biochim. Biophys. Acta 1358:215-220.
    • (1997) Biochim. Biophys. Acta , vol.1358 , pp. 215-220
    • Li, F.1    Liu, J.2    Mayne, R.3    Wu, C.4
  • 16
    • 0026607234 scopus 로고
    • The ANK repeat: A ubiquitous motif involved in macromolecular recognition
    • Michaely, P., and V. Bennett. 1992. The ANK repeat: a ubiquitous motif involved in macromolecular recognition. Trends Cell Biol. 2:127-129.
    • (1992) Trends Cell Biol. , vol.2 , pp. 127-129
    • Michaely, P.1    Bennett, V.2
  • 17
    • 0027374511 scopus 로고
    • The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats
    • Michaely, P., and V. Bennett. 1993. The membrane-binding domain of ankyrin contains four independently folded subdomains, each comprised of six ankyrin repeats. J. Biol. Chem. 268:22703-22709.
    • (1993) J. Biol. Chem. , vol.268 , pp. 22703-22709
    • Michaely, P.1    Bennett, V.2
  • 18
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., H. Teramoto, J. S. Gutkind, and K. M. Yamada. 1996. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135:1633-1642.
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 20
    • 0028817908 scopus 로고
    • Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex
    • Plopper, G. E., H. P. McNamee, L. E. Dike, K. Bojanowski, and D. E. Ingber. 1995. Convergence of integrin and growth factor receptor signaling pathways within the focal adhesion complex. Mol. Biol. Cell 6:1349-1365.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1349-1365
    • Plopper, G.E.1    McNamee, H.P.2    Dike, L.E.3    Bojanowski, K.4    Ingber, D.E.5
  • 22
    • 0027933818 scopus 로고
    • A new Lim protein containing an autoepitope homologous to "senescent cell antigen"
    • Rearden, A. 1994. A new Lim protein containing an autoepitope homologous to "senescent cell antigen." Biochem. Biophys. Res. Commun. 201:1124-1131.
    • (1994) Biochem. Biophys. Res. Commun. , vol.201 , pp. 1124-1131
    • Rearden, A.1
  • 23
    • 0024328167 scopus 로고
    • The fibronectin receptor is organized by extracellular matrix fibronectin: Implications for oncogenic transformation and for cell recognition of fibronectin matrices
    • Roman, J., R. M. LaChance, T. J. Broekelmann, C. J. Kennedy, E. A. Wayner, W. G. Carter, and J. A. McDonald. 1989. The fibronectin receptor is organized by extracellular matrix fibronectin: implications for oncogenic transformation and for cell recognition of fibronectin matrices. J. Cell Biol. 108:2529-2543.
    • (1989) J. Cell Biol. , vol.108 , pp. 2529-2543
    • Roman, J.1    LaChance, R.M.2    Broekelmann, T.J.3    Kennedy, C.J.4    Wayner, E.A.5    Carter, W.G.6    McDonald, J.A.7
  • 24
    • 0027080110 scopus 로고
    • Zyxin and cCRP: Two interactive LIM domain proteins associated with the cytoskeleton
    • Sadler, I., A. W. Crawford, J. W. Michelsen, and M. C. Beckerle. 1992. Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton. J. Cell Biol. 119:1573-1587.
    • (1992) J. Cell Biol. , vol.119 , pp. 1573-1587
    • Sadler, I.1    Crawford, A.W.2    Michelsen, J.W.3    Beckerle, M.C.4
  • 25
    • 0028134697 scopus 로고
    • The LIM domain is a modular protein-binding interface
    • Schmeichel, K. L., and M. C. Beckerle. 1994. The LIM domain is a modular protein-binding interface. Cell 79:211-219.
    • (1994) Cell , vol.79 , pp. 211-219
    • Schmeichel, K.L.1    Beckerle, M.C.2
  • 26
    • 0030814976 scopus 로고    scopus 로고
    • Alpha v beta 3 integrin associates with activated insulin and PDGF beta receptors and potentiates the biological activity of PDGF
    • Schneller, M., K. Vuori, and E. Ruoslahti. 1997. Alpha v beta 3 integrin associates with activated insulin and PDGF beta receptors and potentiates the biological activity of PDGF. EMBO J. 16:5600-5607.
    • (1997) EMBO J. , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 27
    • 0027444230 scopus 로고
    • Integrins in point contacts mediate cell spreading: Factors that regulate integrin accumulation in point contacts vs. focal contacts
    • Tawil, N., P. Wilson, and S. Carbonetto. 1993. Integrins in point contacts mediate cell spreading: factors that regulate integrin accumulation in point contacts vs. focal contacts. J. Cell Biol. 120:261-271.
    • (1993) J. Cell Biol. , vol.120 , pp. 261-271
    • Tawil, N.1    Wilson, P.2    Carbonetto, S.3
  • 28
    • 0031772910 scopus 로고    scopus 로고
    • Nck-2, a novel Src homology 2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase signaling pathways
    • Tu, Y., F. Li, and C. Wu. 1998. Nck-2, a novel Src homology 2/3-containing adaptor protein that interacts with the LIM-only protein PINCH and components of growth factor receptor kinase signaling pathways. Mol. Biol. Cell 9:3367-3382.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3367-3382
    • Tu, Y.1    Li, F.2    Wu, C.3
  • 29
    • 0027966390 scopus 로고
    • Paxillin: A cytoskeletal target for tyrosine kinases
    • Turner, C. E. 1994. Paxillin: a cytoskeletal target for tyrosine kinases. Bioessays 16:47-52.
    • (1994) Bioessays , vol.16 , pp. 47-52
    • Turner, C.E.1
  • 30
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C. E., J. R. Glenney, Jr., and K. Burridge. 1990. Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 111:1059-1068.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney J.R., Jr.2    Burridge, K.3
  • 31
    • 0028641601 scopus 로고
    • Association of insulin receptor substrate-1 with integrins
    • Vuori, K., and E. Ruoslahti. 1994. Association of insulin receptor substrate-1 with integrins. Science 266:1576-1578.
    • (1994) Science , vol.266 , pp. 1576-1578
    • Vuori, K.1    Ruoslahti, E.2
  • 32
    • 0028811671 scopus 로고
    • The cysteine-rich protein family of highly related LIM domain proteins
    • Weiskirchen, R., J. D. Pino, T. Macalma, K. Bister, and M. C. Beckerle. 1995. The cysteine-rich protein family of highly related LIM domain proteins. J. Biol. Chem. 70:28946-28954.
    • (1995) J. Biol. Chem. , vol.70 , pp. 28946-28954
    • Weiskirchen, R.1    Pino, J.D.2    Macalma, T.3    Bister, K.4    Beckerle, M.C.5
  • 34
    • 0031876301 scopus 로고    scopus 로고
    • Expression of the integrin-linked kinase (ILK) in mouse skins: Loss of expression in suprabasal layers of the epidermis and up-regulation by erbB-2
    • Xie, W., F. Li, J. E. Kudlow, and C. Wu. 1998. Expression of the integrin-linked kinase (ILK) in mouse skins: loss of expression in suprabasal layers of the epidermis and up-regulation by erbB-2. Am. J. Pathol. 153:367-372.
    • (1998) Am. J. Pathol. , vol.153 , pp. 367-372
    • Xie, W.1    Li, F.2    Kudlow, J.E.3    Wu, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.