World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos One : Distinct Functional Interactions Between Actin Isoforms and Nonsarcomeric Myosins, Volume 8

By Frischknecht, Friedrich

Click here to view

Book Id: WPLBN0003946897
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos One : Distinct Functional Interactions Between Actin Isoforms and Nonsarcomeric Myosins, Volume 8  
Author: Frischknecht, Friedrich
Volume: Volume 8
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Frischknecht, F. (n.d.). Plos One : Distinct Functional Interactions Between Actin Isoforms and Nonsarcomeric Myosins, Volume 8. Retrieved from http://netlibrary.net/


Description
Description : Despite their near sequence identity, actin isoforms cannot completely replace each other in vivo and show marked differences in their tissue-specific and subcellular localization. Little is known about isoform-specific differences in their interactions with myosin motors and other actin-binding proteins. Mammalian cytoplasmic b- and c-actin interact with nonsarcomeric conventional myosins such as the members of the nonmuscle myosin-2 family and myosin-7A. These interactions support a wide range of cellular processes including cytokinesis, maintenance of cell polarity, cell adhesion, migration, and mechano-electrical transduction. To elucidate differences in the ability of isoactins to bind and stimulate the enzymatic activity of individual myosin isoforms, we characterized the interactions of human skeletal muscle a-actin, cytoplasmic b-actin, and cytoplasmic c-actin with human myosin-7A and nonmuscle myosins-2A, -2B and -2C1. In the case of nonmuscle myosins-2A and -2B, the interaction with either cytoplasmic actin isoform results in 4-fold greater stimulation of myosin ATPase activity than was observed in the presence of a-skeletal muscle actin. Nonmuscle myosin-2C1 is most potently activated by b-actin and myosin-7A by c-actin. Our results indicate that b- and c-actin isoforms contribute to the modulation of nonmuscle myosin-2 and myosin-7A activity and thereby to the spatial and temporal regulation of cytoskeletal dynamics. FRET-based analyses show efficient copolymerization abilities for the actin isoforms in vitro. Experiments with hybrid actin filaments show that the extent of actomyosin coupling efficiency can be regulated by the isoform composition of actin filaments.

 

Click To View

Additional Books


  • Plos One : Molecular Characterization an... (by )
  • Plos One : Evaluation of Chemotherapy Re... (by )
  • Plos One : Transcriptome Analysis of Ski... (by )
  • Plos One : Centrosomal Localization of t... (by )
  • Plos One : Peripheral Blood Mononuclear ... (by )
  • Plos One : Effects of L-dopa During Audi... (by )
  • Plos One : Nitric Oxide Mediates Root K+... (by )
  • Plos One : Akt2 Regulates Metastatic Pot... (by )
  • Plos One : Accumulation of Dna Damage-in... (by )
  • Plos One : Alpha-fetoprotein Promoter-dr... (by )
  • Plos One : Understanding the Social Mean... (by )
  • Plos One : Old-growth Platycladus Orient... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.