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G proteins, phosphoinositides, and actin‐cytoskeleton in the control of cancer growth
Author(s) -
Maruta Hiroshi,
He Hong,
Tikoo Anjali,
Vuong Thao,
NurEKamal MSA
Publication year - 1999
Publication title -
microscopy research and technique
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 118
eISSN - 1097-0029
pISSN - 1059-910X
DOI - 10.1002/(sici)1097-0029(19991001)47:1<61::aid-jemt6>3.0.co;2-y
Subject(s) - cdc42 , microbiology and biotechnology , actin cytoskeleton , actin , cytoskeleton , motility , gtpase , biology , myosin , actin remodeling , actin binding protein , cell , biochemistry
Almost three decades have passed since actin‐cytoskeleton (acto‐myosin complex) was first discovered in non‐muscle cells. A combination of cell biology, biochemistry, and molecular biology has revealed the structure and function of many actin‐binding proteins and their physiological role in the regulation of cell motility, shape, growth, and malignant transformation. As molecular oncologists, we would like to review how the function of actin‐cytoskeleton is regulated through Ras/Rho family GTPases‐ or phosphoinosites‐mediated signaling pathways, and how malignant transformation is controlled by actin/phosphoinositides‐binding proteins or drugs that block Rho/Rac/CDC42 GTPases‐mediated signaling pathways. Microsc. Res. Tech. 47:61–66, 1999. © 1999 Wiley‐Liss, Inc.