How are the cellular functions of myosin V1 regulated within the cell?

被引：71

作者：

Buss, Folma ^{[2
]}

Kendrick-Jones, John ^{[1
]}

机构：

[1] MRC, Mol Biol Lab, Cambridge CB2 2QH, England

[2] Univ Cambridge, Cambridge Inst Med Res, Cambridge CB2 2XY, England

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2008年 / 369卷 / 01期

基金：

英国惠康基金; 英国医学研究理事会;

关键词：

motor proteins; myosin VI; actin; cytoskeleton; PtdIns(4,5)P-2; membrane trafficking; myosin phosphorylation; optineurin; Dab2; GIPC;

D O I：

10.1016/j.bbrc.2007.11.150

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

This review, dedicated to the memory of Professor Setsuro Ebashi, focuses on our current work investigating the cellular functions and regulation of the unique unconventional motor, myosin VI. This myosin, unlike all the other myosins so far studied, moves towards the minus end of actin filaments and has been implicated in a wide range of cellular processes such as endocytosis, exocytosis, cell migration, cell division and cytokinesis. Myosin VI's involvement in these cellular pathways is mediated by its interaction with specific adaptor proteins and is regulated by multiple regulatory signals and modifications such as calcium ions, PtdIns(4,5)P-2 (PIP2) and phosphorylation. Understanding the functions of myosin VI within the cell and how it is regulated is now of utmost importance given the recent observations that it is associated with a number of human disorders such as deafness and cancers. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：165 / 175

页数：11

共 106 条

[41] MOLECULAR EVOLUTION OF THE MYOSIN FAMILY - RELATIONSHIPS DERIVED FROM COMPARISONS OF AMINO-ACID-SEQUENCES [J].

GOODSON, HV ;

SPUDICH, JA .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1993, 90 (02) :659-663

[42] Interactions of the low density lipoprotein receptor gene family with cytosolic adaptor and scaffold proteins suggest diverse biological functions in cellular communication and signal transduction [J].

Gotthardt, M ;

Trommsdorff, M ;

Nevitt, MF ;

Shelton, J ;

Richardson, JA ;

Stockinger, W ;

Nimpf, J ;

Herz, J .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (33) :25616-25624

[43]

GREASER ML, 1971, J BIOL CHEM, V246, P4226

[44] THE TRANS GOLGI NETWORK - SORTING AT THE EXIT SITE OF THE GOLGI-COMPLEX [J].

GRIFFITHS, G ;

SIMONS, K .

SCIENCE, 1986, 234 (4775) :438-443

[45] Rho GTPases and the actin cytoskeleton [J].

Hall, A .

SCIENCE, 1998, 279 (5350) :509-514

[46] STUDIES ON TROPONIN [J].

HARTSHORNE, DJ ;

THEINER, M ;

MUELLER, H .

BIOCHIMICA ET BIOPHYSICA ACTA, 1969, 175 (02) :320-+

[47]

HARTSHORNE DJ, 1980, HDB PHYSL CARDIOVASC, P93

[48] PORCINE MYOSIN-VI - CHARACTERIZATION OF A NEW MAMMALIAN UNCONVENTIONAL MYOSIN [J].

HASSON, T ;

MOOSEKER, MS .

JOURNAL OF CELL BIOLOGY, 1994, 127 (02) :425-440

[49] FIP-2, a coiled-coil protein, links Huntingtin to Rab8 and modulates cellular morphogenesis [J].

Hattula, K ;

Peränen, J .

CURRENT BIOLOGY, 2000, 10 (24) :1603-1606

[50] GIPC binds to the human lutropin receptor (hLHR) through an unusual PDZ domain binding motif, and it regulates the sorting of the internalized human choriogonadotropin and the density of cell surface hLHR [J].

Hirakawa, T ;

Galet, C ;

Kishi, M ;

Ascoli, M .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (49) :49348-49357

← 1 2 3 4 5 6 7 8 9 10 →