Premium
Molecular shape and self‐association of vinculin and metavinculin
Author(s) -
Molony Leslie,
Burridge Keith
Publication year - 1985
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240290104
Subject(s) - vinculin , biophysics , adhesion , electron microscope , chemistry , cell adhesion , biology , physics , optics , organic chemistry
Vinculin, a 130,000‐dalton protein localized to adhesion plaques, and metavinculin, a 150,‐000 dalton protein closely related to vinculin, have been studied using rotary shadowing and electron microscopy. Both proteins have globular head regions attached to rod‐shaped tail domains. Vinculin and metavinculin also both form complexes consisting of four to six individual molecules. These multimers are formed by head‐to‐head as well as tail‐to‐tail interactions. Talin, another protein which has been localized to adhesion plaques and binds to both vinculin and metavinculin, has also been investigated using shadowing techniques. Talin is an elongated, flexible molecule in high ionic strength buffers, as shown here by rotary shadowing and negative stain electron microscopy.