Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Search research articles

Related Experiment Videos

The functional importance of multiple actin isoforms.

P A Rubenstein¹

¹Department of Biochemistry, University of Iowa College of Medicine, Iowa City 52242.

Bioessays : News and Reviews in Molecular, Cellular and Developmental Biology

|July 1, 1990

Summary

This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

The structure of nonvertebrate actin: implications for the ATP hydrolytic mechanism.

Proceedings of the National Academy of Sciences of the United States of America·2003

Same author

F-actin-like ATPase activity in a polymerization-defective mutant yeast actin (V266G/L267G).

The Journal of biological chemistry·2001

Same author

Tropomyosin-dependent filament formation by a polymerization-defective mutant yeast actin (V266G,L267G).

The Journal of biological chemistry·2000

Same author

Interaction of the gonococcal porin P.IB with G- and F-actin.

Biochemistry·2000

Same author

Cross-linking constraints on F-actin structure.

Journal of molecular biology·2000

Same author

Structural transition at actin's N-terminus in the actomyosin cross-bridge cycle.

Biochemistry·2000

Same journal

AI in Genomics: From Variant Calling to Multi-Omics Integration.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026

Same journal

Rethinking One Health: Microbial Foundations for Ecological Governance.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026

Same journal

Biobanked Liver Organoids: A Roadmap for Precision Hepatology.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026

Same journal

The Temporal Architecture of Human Cells: Organelle Clocks and Distributed Circadian Time.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026

Same journal

Opposing Activity at the Apical Surface: An Antagonistic Collaboration Between Crumbs and Myosin II Determines Organ Shape.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026

Same journal

Hidden Fungal DNA Structures May Shape Sequencing Outcomes.

BioEssays : news and reviews in molecular, cellular and developmental biology·2026

See all related articles

Multiple actin protein forms (isoactins) exist, with tissue-specific expression suggesting distinct functions. Their precise necessity in cellular processes remains under investigation.

Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Actin is a crucial protein for cell structure, motility, and force generation in muscle and nonmuscle cells.
Multiple actin forms, known as isoactins, arise from different genes and exhibit distinct yet similar amino acid sequences.
Isoactin expression is tissue-specific across species, implying functional significance and quantifiable differences in vitro.

Purpose of the Study:

To explore the functional importance and tissue-specific distribution of various actin isoforms.
To investigate the differential localization of isoactins within muscle cells, including associations with costameres, mitochondria, and neuromuscular junctions.
To examine evidence for specific isoactin roles in microvascular pericytes and the intestinal brush border.

Main Methods:

Related Experiment Videos

Comparative analysis of isoactin amino acid sequences.
In vitro characterization of isoactin behavior.
Histological and biochemical localization studies in various cell types.

Main Results:

Isoactins exhibit conserved, tissue-specific expression patterns across species.
Differential distribution of isoactins observed within muscle cells, with specific associations noted.
Evidence suggests specialized roles for isoactins in pericytes and intestinal brush borders.

Conclusions:

The tissue-specific expression of isoactins strongly suggests specialized functions.
While differential localization and associations are observed, the essentiality of specific isoactins for particular cellular functions requires further conclusive demonstration.