Phosphorylation of septin 3 on Ser-91 by cGMP-dependent protein kinase-1 in nerve terminals

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dc.contributor.authorXue, Jing
dc.contributor.authorMilburn, Peter J
dc.contributor.authorHanna, Bernadette
dc.contributor.authorGraham, Mark E
dc.contributor.authorRostas, John A P
dc.contributor.authorRobinson, Phillip J
dc.date.accessioned2015-12-13T22:51:32Z
dc.date.available2015-12-13T22:51:32Z
dc.date.issued2004
dc.date.updated2015-12-11T10:45:43Z
dc.description.abstractThe septins are a family of GTPase enzymes required for cytokinesis and play a role in exocytosis. Among the ten vertebrate septins, Sept5 (CDCrel-1) and Sept3 (G-septin) are primarily concentrated in the brain, wherein Sept3 is a substrate for PKG-I (cGMP-dependent protein kinase-I) in nerve terminals. There are two motifs for potential PKG-I phosphorylation in Sept3, Thr-55 and Ser-91, but phosphoamino acid analysis revealed that the primary site is a serine. Derivatization of phosphoserine to S-propylcysteine followed by N-terminal sequence analysis revealed Ser-91 as a major phosphorylation site. Tandem MS revealed a single phosphorylation site at Ser-91. Substitution of Ser-91 with Ala in a synthetic peptide abolished phosphorylation. Mutation of Ser-91 to Ala in recombinant Sept3 also abolished PKG phosphorylation, confirming that Ser-91 is the major site in vitro. Antibodies raised against a peptide containing phospho-Ser-91 detected phospho-Sept3 only in the cytosol of nerve terminals, whereas Sept3 was located in a peripheral membrane extract. Therefore Sept3 is phosphorylated on Ser-91 in nerve terminals and its phosphorylation may contribute to the regulation of its subcellular localization in neurons.
dc.identifier.issn0264-6021
dc.identifier.urihttp://hdl.handle.net/1885/81128
dc.publisherPortland Press
dc.sourceBiochemical Journal
dc.subjectKeywords: Polypeptides; Proteins; Substitution reactions; Substrates; Phosphorylation; Vertebrate septins; Biochemistry; brain enzyme; cyclic GMP dependent protein kinase; cyclic GMP dependent protein kinase I; cysteine derivative; guanosine triphosphatase; phospho cGMP; cGMP-dependent protein kinase (PKG); Protein phosphorylation; Sept3; Septins; Synaptosomes
dc.titlePhosphorylation of septin 3 on Ser-91 by cGMP-dependent protein kinase-1 in nerve terminals
dc.typeJournal article
local.bibliographicCitation.lastpage760
local.bibliographicCitation.startpage753
local.contributor.affiliationXue, Jing, Children's Medical Research Institute
local.contributor.affiliationMilburn, Peter J, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHanna, Bernadette, Children's Medical Research Institute
local.contributor.affiliationGraham, Mark E, Children's Medical Research Institute
local.contributor.affiliationRostas, John A P, University of Newcastle
local.contributor.affiliationRobinson, Phillip J, Children's Medical Research Institute
local.contributor.authoremailu8707729@anu.edu.au
local.contributor.authoruidMilburn, Peter J, u8707729
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.absfor060104 - Cell Metabolism
local.identifier.absfor110106 - Medical Biochemistry: Proteins and Peptides (incl. Medical Proteomics)
local.identifier.ariespublicationMigratedxPub9473
local.identifier.citationvolume381
local.identifier.doi10.1042/BJ20040455
local.identifier.scopusID2-s2.0-4344573131
local.identifier.uidSubmittedByMigrated
local.type.statusPublished Version

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