alexa Interaction of myristoylated alanine-rich protein kinase C substrate (MARCKS) with membrane phospholipids.
Bioinformatics & Systems Biology

Bioinformatics & Systems Biology

Journal of Glycomics & Lipidomics

Author(s): Taniguchi H, Manenti S

Abstract Share this page

Abstract A major in vivo substrate of Ca(2+)-phospholipid-dependent protein kinase (MARCKS) shows phosphorylation-dependent translocation between the cytoplasmic and the membrane fractions. The mechanism of the translocation was studied with purified MARCKS and various membranes. MARCKS was found to bind to pure phospholipid membranes as well as to the synaptic vesicle membranes. Although the interaction of MARCKS with the latter was phosphorylation-dependent, phosphorylation by protein kinase C showed no significant effect on the binding to the phosphatidylcholine liposomes. However, when phosphatidylserine was included in the membranes, the association became phosphorylation-dependent. A synthetic phosphorylation domain peptide showed a similar phosphorylation-dependent interaction with the negatively charged liposomes. Phosphatidylserine but not phosphatidylcholine inhibited phosphorylation of MARCKS by protein kinase C. MARCKS seems to bind to the biomembranes through two binding sites: the N-terminal myristoyl moiety and the basic phosphorylation domain of amphiphilic nature. Phosphorylation of this domain lowers its affinity to phosphatidylserine and makes the whole molecule strongly negatively charged, which causes its dissociation from the membranes.
This article was published in J Biol Chem and referenced in Journal of Glycomics & Lipidomics

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Relevant Topics

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords