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Volumn 1823, Issue 6, 2012, Pages 1058-1067

The PDZ-binding motif of MCC is phosphorylated at position -1 and controls lamellipodia formation in colon epithelial cells

Author keywords

Lamellipodia; MCC; Myosin IIB; PDZ; PDZ binding motif; Scrib

Indexed keywords

CELL PROTEIN; MUTATED IN COLORECTAL CANCER PROTEIN; MYOSIN IIB; PROTEIN SCRIB; UNCLASSIFIED DRUG;

EID: 84860312399     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2012.03.011     Document Type: Article
Times cited : (22)

References (27)
  • 2
    • 53649084334 scopus 로고    scopus 로고
    • Mutated in colorectal cancer, a putative tumor suppressor for serrated colorectal cancer, selectively represses beta-catenin-dependent transcription
    • Fukuyama R., Niculaita R., Ng K.P., Obusez E., Sanchez J., Kalady M., Aung P.P., Casey G., Sizemore N. Mutated in colorectal cancer, a putative tumor suppressor for serrated colorectal cancer, selectively represses beta-catenin-dependent transcription. Oncogene 2008, 27:6044-6055.
    • (2008) Oncogene , vol.27 , pp. 6044-6055
    • Fukuyama, R.1    Niculaita, R.2    Ng, K.P.3    Obusez, E.4    Sanchez, J.5    Kalady, M.6    Aung, P.P.7    Casey, G.8    Sizemore, N.9
  • 7
    • 0032568655 scopus 로고    scopus 로고
    • SMART, a simple modular architecture research tool: identification of signaling domains
    • Schultz J., Milpetz F., Bork P., Ponting C.P. SMART, a simple modular architecture research tool: identification of signaling domains. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:5857-5864.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 5857-5864
    • Schultz, J.1    Milpetz, F.2    Bork, P.3    Ponting, C.P.4
  • 9
    • 34147094240 scopus 로고    scopus 로고
    • The tumour-suppressor Scribble dictates cell polarity during directed epithelial migration: regulation of Rho GTPase recruitment to the leading edge
    • Dow L.E., Kauffman J.S., Caddy J., Zarbalis K., Peterson A.S., Jane S.M., Russell S.M., Humbert P.O. The tumour-suppressor Scribble dictates cell polarity during directed epithelial migration: regulation of Rho GTPase recruitment to the leading edge. Oncogene 2007, 26:2272-2282.
    • (2007) Oncogene , vol.26 , pp. 2272-2282
    • Dow, L.E.1    Kauffman, J.S.2    Caddy, J.3    Zarbalis, K.4    Peterson, A.S.5    Jane, S.M.6    Russell, S.M.7    Humbert, P.O.8
  • 11
    • 0012927828 scopus 로고    scopus 로고
    • PDZ domain proteins: plug and play!
    • Nourry C., Grant S.G., Borg J.P. PDZ domain proteins: plug and play!. Sci. STKE 2003, 2003:RE7.
    • (2003) Sci. STKE , vol.2003
    • Nourry, C.1    Grant, S.G.2    Borg, J.P.3
  • 13
    • 32144463131 scopus 로고    scopus 로고
    • Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility
    • Morris J.R., Pangon L., Boutell C., Katagiri T., Keep N.H., Solomon E. Genetic analysis of BRCA1 ubiquitin ligase activity and its relationship to breast cancer susceptibility. Hum. Mol. Genet. 2006, 15:599-606.
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 599-606
    • Morris, J.R.1    Pangon, L.2    Boutell, C.3    Katagiri, T.4    Keep, N.H.5    Solomon, E.6
  • 14
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: structure, specificity, and modification
    • Lee H.J., Zheng J.J. PDZ domains and their binding partners: structure, specificity, and modification. Cell Commun. Signal. 2010, 8:8.
    • (2010) Cell Commun. Signal. , vol.8 , pp. 8
    • Lee, H.J.1    Zheng, J.J.2
  • 16
    • 0034647505 scopus 로고    scopus 로고
    • Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display
    • Fuh G., Pisabarro M.T., Li Y., Quan C., Lasky L.A., Sidhu S.S. Analysis of PDZ domain-ligand interactions using carboxyl-terminal phage display. J. Biol. Chem. 2000, 275:21486-21491.
    • (2000) J. Biol. Chem. , vol.275 , pp. 21486-21491
    • Fuh, G.1    Pisabarro, M.T.2    Li, Y.3    Quan, C.4    Lasky, L.A.5    Sidhu, S.S.6
  • 18
    • 77649103340 scopus 로고    scopus 로고
    • Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading
    • Betapudi V. Myosin II motor proteins with different functions determine the fate of lamellipodia extension during cell spreading. PLoS One 2010, 5:e8560.
    • (2010) PLoS One , vol.5
    • Betapudi, V.1
  • 20
    • 21644467031 scopus 로고    scopus 로고
    • PAK1 regulates myosin II-B phosphorylation, filament assembly, localization and cell chemotaxis
    • Even-Faitelson L., Rosenberg M., Ravid S. PAK1 regulates myosin II-B phosphorylation, filament assembly, localization and cell chemotaxis. Cell. Signal. 2005, 17:1137-1148.
    • (2005) Cell. Signal. , vol.17 , pp. 1137-1148
    • Even-Faitelson, L.1    Rosenberg, M.2    Ravid, S.3
  • 21
    • 33745625368 scopus 로고    scopus 로고
    • PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly
    • Even-Faitelson L., Ravid S. PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly. Mol. Biol. Cell 2006, 17:2869-2881.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2869-2881
    • Even-Faitelson, L.1    Ravid, S.2
  • 22
    • 78549241917 scopus 로고    scopus 로고
    • Myosin light chain mono- and di-phosphorylation differentially regulate adhesion and polarity in migrating cells
    • Vicente-Manzanares M., Horwitz A.R. Myosin light chain mono- and di-phosphorylation differentially regulate adhesion and polarity in migrating cells. Biochem. Biophys. Res. Commun. 2010, 402:537-542.
    • (2010) Biochem. Biophys. Res. Commun. , vol.402 , pp. 537-542
    • Vicente-Manzanares, M.1    Horwitz, A.R.2
  • 23
    • 0030604722 scopus 로고    scopus 로고
    • Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ
    • Doyle D.A., Lee A., Lewis J., Kim E., Sheng M., MacKinnon R. Crystal structures of a complexed and peptide-free membrane protein-binding domain: molecular basis of peptide recognition by PDZ. Cell 1996, 85:1067-1076.
    • (1996) Cell , vol.85 , pp. 1067-1076
    • Doyle, D.A.1    Lee, A.2    Lewis, J.3    Kim, E.4    Sheng, M.5    MacKinnon, R.6
  • 24
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
    • Wang S., Raab R.W., Schatz P.J., Guggino W.B., Li M. Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett. 1998, 427:103-108.
    • (1998) FEBS Lett. , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 25
    • 0037166247 scopus 로고    scopus 로고
    • + exchanger regulatory factor interaction with the β2 adrenergic and platelet-derived growth factor receptors
    • + exchanger regulatory factor interaction with the β2 adrenergic and platelet-derived growth factor receptors. J. Biol. Chem. 2002, 277:18973-18978.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18973-18978
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3
  • 27
    • 0035827518 scopus 로고    scopus 로고
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator
    • + exchanger regulatory factor PDZ1 interaction with the carboxyl-terminal region of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 2001, 276:19683-19686.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19683-19686
    • Karthikeyan, S.1    Leung, T.2    Ladias, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.