메뉴 건너뛰기




Volumn 362, Issue 1, 2002, Pages 1-12

Cross-talk unfolded: MARCKS proteins

Author keywords

Actin; Calmodulin; Membranes; PIP2; PKC

Indexed keywords

BIOLOGICAL MEMBRANES; BRAIN; CELLS; ENZYME KINETICS; POLYMERIZATION;

EID: 0037083896     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3620001     Document Type: Review
Times cited : (288)

References (125)
  • 3
    • 0023764824 scopus 로고
    • The molecular heterogeneity of protein kinase C and its implications for cellular regulation
    • (1988) Nature (London) , vol.334 , pp. 661-665
    • Nishizuka, Y.1
  • 4
    • 0035951789 scopus 로고    scopus 로고
    • 2+-dependent cell signalling through calmodulin-activated protein phosphatase and protein kinases
    • (2001) J. Biol. Chem. , vol.276 , pp. 2311-2312
    • Stull, J.T.1
  • 6
    • 2042442261 scopus 로고    scopus 로고
    • Erratum (2000) Trends Cell Biol. 10, 428
  • 7
    • 0026472164 scopus 로고
    • The MARCKS brothers: A family of protein kinase C substrates
    • (1992) Cell , vol.71 , pp. 713-716
    • Aderem, A.1
  • 9
    • 0033578731 scopus 로고    scopus 로고
    • Characterization of the targeting, binding, and phosphorylation site domains of an A kinase anchor protein and a rnyristoylated alanine-rich C kinase substrate-like analog that are encoded by a single gene
    • (1999) J. Biol. Chem. , vol.274 , pp. 27201-27210
    • Rossi, E.A.1    Li, Z.2    Feng, H.3    Rubin, C.S.4
  • 18
    • 0029162389 scopus 로고
    • A role for MARCKS, the α isozyme of protein kinase C and myosin I in zymosan phagocytosis by macrophages
    • (1995) J. Exp. Med. , vol.182 , pp. 829-840
    • Allen, L.H.1    Aderem, A.2
  • 20
    • 0029053995 scopus 로고
    • Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein. Mutational analysis provides evidence for complex interactions
    • (1995) J. Biol. Chem. , vol.270 , pp. 13436-13445
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 21
    • 0028909477 scopus 로고
    • Protein kinase C regulates MARCKS cycling between the plasma membrane and lysosomes in fibroblasts
    • (1995) EMBO J. , vol.14 , pp. 1109-1121
    • Allen, L.A.1    Aderem, A.2
  • 30
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 31
    • 0033552652 scopus 로고    scopus 로고
    • Protein myristoylation in protein-lipid and protein-protein interactions
    • (1999) Biophys. Chem. , vol.82 , pp. 129-137
    • Taniguchi, H.1
  • 39
    • 0029831440 scopus 로고    scopus 로고
    • Myristoylation-dependent and electrostatic interactions exert independent effects on the membrane association of the Myristoylated Alanine-rich C-kinase Substrate protein in intact cells
    • (1996) J. Biol. Chem. , vol.271 , pp. 23424-23430
    • Swierczynski, S.L.1    Blackshear, P.J.2
  • 44
    • 0035943628 scopus 로고    scopus 로고
    • Overexpression of the myristoylated alanine-rich C-kinase substrate inhibits cell adhesion to extracellular matrix components
    • (2001) J. Biol. Chem. , vol.276 , pp. 32264-32273
    • Spizz, G.1    Blackshear, P.J.2
  • 46
    • 0029921472 scopus 로고    scopus 로고
    • Membrane structure of the protein kinase C and calmodulin binding domain of Myristoylated Alanine Rich C Kinase Substrate determined by site-directed spin labeling
    • (1996) Biochemistry , vol.35 , pp. 2917-2925
    • Qin, Z.1    Cafiso, D.S.2
  • 47
    • 0039182142 scopus 로고    scopus 로고
    • Interactions controlling the membrane binding of basic protein domains: Phenylalanine and the attachment of the myristoylated alanine-rich C-kinase substrate protein to interfaces
    • (1999) Biochemistry , vol.38 , pp. 12527-12536
    • Victor, K.1    Jacob, J.2    Cafiso, D.S.3
  • 52
    • 0035918191 scopus 로고    scopus 로고
    • In vivo interaction between dynamitin and MacMARCKS detected by the fluorescent resonance energy transfer method
    • (2001) J. Biol. Chem. , vol.276 , pp. 12879-12884
    • Jin, T.1    Yue, L.2    Li, J.3
  • 55
    • 0032519778 scopus 로고    scopus 로고
    • Binding of MARCKS (myristoylated alanine-rich C kinase substrate)-related protein (MRP) to vesicular phospholipid membranes
    • (1998) Biochem. J. , vol.330 , pp. 5-11
    • Vergères, G.1    Ramsden, J.J.2
  • 85
    • 0034677631 scopus 로고    scopus 로고
    • 3: Complex roles at the cell surface
    • (2000) Cell , vol.100 , pp. 603-666
    • Czech, M.P.1
  • 86
    • 0032407241 scopus 로고    scopus 로고
    • Phosphoinositide lipids as signaling molecules: Common themes for signal transduction, cytoskeletal regulation and membrane trafficking
    • (1998) Annu. Rev. Cell Dev. Biol. , vol.14 , pp. 231-264
    • Martin, T.F.J.1
  • 87
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 100
    • 0030036555 scopus 로고    scopus 로고
    • Chronic lithium-induced down-regulation of MARCKS in immortalized hippocampal cells: Potentiation by muscarinic receptor activation
    • (1996) J. Neurochem , vol.67 , pp. 767-777
    • Watson, D.G.1    Lenox, R.H.2
  • 103
  • 109
    • 0030070806 scopus 로고    scopus 로고
    • Protein klnase C-mediated phosphorylation of the myristoylated alanine-rich C-kinase substrate protects it from specific proteolytic cleavage
    • (1996) J. Biol. Chem. , vol.271 , pp. 553-562
    • Spizz, G.1    Blackshear, P.J.2
  • 122
    • 0028334631 scopus 로고
    • Myristoylated alanine-rich C kinase substrate (MARCKS), a major protein kinase C substrate, is an in vivo substrate of proline-directed protein kinase(s). A mass spectroscopic analysis of the post-translational modifications
    • (1994) J. Biol. Chem. , vol.269 , pp. 18299-18302
    • Taniguchi, H.1    Manenti, S.2    Suzuki, M.3    Titani, K.4
  • 123
    • 0032548845 scopus 로고    scopus 로고
    • The C-terminal conserved domain of MARCKS is phosphorylated in vivo by proline-directed protein kinase. Application of ion trap mass spectrometry to the determination of protein phosphorylation sites
    • (1998) J. Biol. Chem. , vol.273 , pp. 4367-4371
    • Yamauchi, E.1    Kiyonami, R.2    Kanai, M.3    Taniguchi, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.