Interaction of S100a0 protein with the actin capping protein, CapZ: characterization of a putative S100a0 binding site in CapZ alpha-subunit

S100a0, a Ca2+-binding protein expressed predominantly in cardiac and skeletal muscle tissues, was demonstrated by chemical cross-linking to interact in a Ca2+ -dependent manner with the actin capping protein CapZ. TRTK-12, a peptide contained within the COOH-terminal region of CapZalpha, inhibited...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1996-04, Vol.221 (1), p.46-50
Main Authors: Ivanenkov, V V, Dimlich, R V, Jamieson, Jr, G A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Binding Sites
Calcium - metabolism
CapZ Actin Capping Protein
Cattle
Microfilament Proteins
Molecular Sequence Data
Muscle Proteins - metabolism
Phosphatidylinositol Phosphates - metabolism
Protein Binding
S100 Proteins - metabolism
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:S100a0, a Ca2+-binding protein expressed predominantly in cardiac and skeletal muscle tissues, was demonstrated by chemical cross-linking to interact in a Ca2+ -dependent manner with the actin capping protein CapZ. TRTK-12, a peptide contained within the COOH-terminal region of CapZalpha, inhibited S100a0: CapZ interaction in a dose-dependent manner. TRTK-12 was shown by cross-linking to bind S100a0 in the presence of Ca2+, and by fluorescence spectrophotometry to interact in a saturable manner with the anionic phospholipid and a regulator of CapZ activity, phosphatidylinositol 4-monophosphate; but not with the neutral phospholipid, phosphatidylcholine. These data suggest S100a0 and polyphosphoinositides bind to the same COOH-terminal region of CapZalpha, thus potentially modulating CapZ activity.
ISSN:0006-291X