These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Coordinated regulation of synapsin I interaction with F-actin by Ca2+/calmodulin and phosphorylation: inhibition of actin binding and bundling.
    Author: Goold R, Chan KM, Baines AJ.
    Journal: Biochemistry; 1995 Feb 14; 34(6):1912-20. PubMed ID: 7849051.
    Abstract:
    The synapsins are a family of synaptic vesicle phosphoproteins whose role seems to be to limit the availability of small synaptic vesicles for exocytosis by linking them to the cytoskeleton. One member of the family, synapsin I, has been shown to bind calmodulin in a Ca(2+)-dependent manner. In this study, we have examined whether or not calmodulin can regulate one of the activities of synapsin I, namely, its interaction with F-actin. Synapsin I is an actin bundling protein: this activity is controlled by phosphorylation. Here we show that calmodulin in the presence of Ca2+ is a competitive inhibitor of both actin binding and bundling by synapsin I. Under the conditions of our assay (0.45 microM synapsin I, 4 microM F-actin), half-maximal inhibition of actin binding and bundling by unphosphorylated synapsin I was found with 4.3 and 3.7 microM calmodulin, respectively. The actin binding activity of synapsin I phosphorylated by cAMP-dependent protein kinase or by calmodulin-dependent protein kinase II showed similar sensitivity to calmodulin inhibition to unphosphorylated synapsin I. However, inhibition of bundling was potentiated. Half-maximal inhibition of bundling by synapsin I phosphorylated by cAMP-dependent kinase was achieved at approximately 0.5 microM calmodulin. Half-maximal inhibition of bundling by synapsin I phosphorylated by calmodulin-dependent protein kinase II was achieved at less than 0.2 microM calmodulin, although the maximum binding under the conditions of the assay was lower.(ABSTRACT TRUNCATED AT 250 WORDS)
    [Abstract] [Full Text] [Related] [New Search]