Severe developmental defects in Dictyostelium null mutants for actin-binding proteins.

Abstract:

:The actin cytoskeleton is implicated in many cellular processes, such as cell adhesion, locomotion, contraction and cytokinesis, which are central to any development. The extent of polymerization, cross-linking, and bundling of actin is regulated by several actin-binding proteins. Knock-out mutations in these proteins have revealed in many cases only subtle, if any, defects in development, suggesting that the actin system is redundant, with multiple proteins sharing overlapping functions. The apparent redundancy may, however, reflect limitations of available laboratory assays in assessing the developmental role of a given protein. By using a novel assay, which reproduces conditions closer to the natural ones, we have re-examined the effects of disruption of many actin-binding proteins, and show here that deletion of alpha-actinin, interaptin, synexin, 34-kDa actin-bundling protein, and gelation factor affect to varying degrees the efficiency of Dictyostelium cells to complete development and form viable spores. No phenotypic defects were found in hisactophilin or comitin null mutants.

journal_name

Mech Dev

authors

Ponte E,Rivero F,Fechheimer M,Noegel A,Bozzaro S

doi

10.1016/s0925-4773(99)00292-0

subject

Has Abstract

pub_date

2000-03-01 00:00:00

pages

153-61

issue

1-2

eissn

0925-4773

issn

1872-6356

pii

S0925-4773(99)00292-0

journal_volume

91

pub_type

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