An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin-Reference-Cited by-同舟云学术

An actin-binding site containing a conserved motif of charged amino acid residues is essential for the morphogenic effect of villin

Published:1992-07 Issue:1 Volume:70 Page:81-92
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Friederich Evelyne,Vancompernolle Katie,Huet Christian,Goethals Marc,Finidori Joëlle,Vandekerckhove Joël,Louvard Daniel

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference45 articles.

1. The F-actin capping proteins of Physarum polycephalum cap 42a is very similar, if not identical, to fragmin and is structurally and functionally very homologous to gelsolin; cap 42b is Physarum actin;Ampe;EMBO J.,1987

2. Severin, gelsolin, and villin share a homologous sequence in regions presumed to contain F-actin severing domains;André;J. Biol. Chem.,1988

3. Sequence of human villin: a large duplicated domain homologous with other actin-severing proteins and a unique small carboxy-terminal domain related to villin specificity;Arpin;J. Cell Biol.,1988

4. Villin sequence and peptide map identify six homologous domains;Bazari,1988

5. Alterations in the phenotype of plant cells studied by NH2-terminal amino acid-sequence analysis of proteins electroblotted from two-dimensional gel-separated total extracts;Bauw,1987

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