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PMID: 7929588 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Differential localization and sequence analysis of capping protein beta-subunit isoforms of vertebrates.

The Journal of cell biology ·Vol. 127 ·No. 2 ·1994-10-00 ·Pages 453-65

Schafer DA, Korshunova YO, Schroer TA, Cooper JA

Abstract

Capping protein nucleates the assembly of actin filaments and stabilizes actin filaments by binding to their barbed ends. We describe here a novel isoform of the beta subunit of chicken capping protein, the beta 2 isoform, which arises by alternative splicing. The chicken beta 1 isoform and the beta 2 isoform are identical in their amino acid sequence except for a short region at the COOH terminus; this region of the beta subunit has been implicated in binding actin. Human and mouse cDNAs of the beta 1 and beta 2 isoforms also were isolated and among these vertebrates, the COOH-terminal region of each isoform is highly conserved. In contrast, comparison of the sequences of the vertebrate beta subunit COOH-termini to those of lower eukaryotes shows no similarities. The beta 2 isoform is the predominant isoform of nonmuscle tissues and the beta 1 isoform, which was first characterized in studies of capping protein from chicken muscle, is the predominant isoform of muscle tissues, as shown by immunoblots probed with isoform-specific antibodies and by RNAse protection analysis of mRNAs. The beta 2 isoform also is a component of dynactin complex from brain, which contains the actin-related protein Arp1. Both beta-subunit isoforms are expressed in cardiac muscle but they have non-overlapping subcellular distributions. The beta 1 isoform is at Z-discs of myofibrils, and the beta 2 isoform is enriched at intercalated discs; in cardiac myocytes grown in culture, the beta 2 isoform also is a component of cell-cell junctions and at sites where myofibrils contact the sarcolemma. The biochemical basis for the differential distribution of capping protein isoforms is likely due to interaction with specific proteins at Z-discs and cell-cell junctions, or to preferential association with different actin isoforms. Thus, vertebrates have developed isoforms of capping protein that associate with distinct actin-filament arrays.

MeSH Terms
Actin Depolymerizing Factors Actins/metabolism Amino Acid Sequence Animals Base Sequence Brain Chemistry Cells, Cultured Chickens DNA, Complementary/chemistry,genetics Destrin Dynactin Complex Gizzard, Avian/chemistry Humans Intercellular Junctions/chemistry Liver/chemistry Mice Microfilament Proteins/analysis,chemistry,genetics,metabolism Microtubule Proteins/chemistry Microtubule-Associated Proteins Molecular Sequence Data Muscle, Skeletal/chemistry Myocardium/chemistry,cytology RNA, Messenger/genetics,metabolism Sequence Alignment Sequence Analysis
Chemicals
Actin Depolymerizing Factors Actins DNA, Complementary Destrin Dynactin Complex Microfilament Proteins Microtubule Proteins Microtubule-Associated Proteins RNA, Messenger
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Schafer D A
Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110.
Korshunova Y O
Schroer T A
Cooper J A
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.127.2.453
Published
1994-10-00
Pages
453-65
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2120197
Subset
IM
Grants
NIGMS NIH HHS · GM38852 · United States
NIGMS NIH HHS · GM44589 · United States
Databases
GENBANK
D12250, U07826, U10406, U10407
External Links
PubMed source DOI: 10.1083/jcb.127.2.453 PMC Full Text View journal details
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