Linked Life Data

15150837

Source:http://linkedlifedata.com/resource/pubmed/id/15150837

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2004-5-19
pubmed:abstractText
Septins constitute a family of conserved proteins that are required for cytokinesis in a wide range of organisms. Most cells express a set of septin proteins and these are found to assemble into hetero-oligomeric septin complexes that appear filamentous. However, the mechanisms controlling the function and polymerization of septins are not known. We therefore examined the possibility that septins could be post-translationally modified by phosphorylation. We present herein a combined theoretical and experimental approach for the analysis of Septin 2 (Sept2) monophosphorylation in vivo. We purified and characterized the human recombinant Sept2, a 45-kDa protein, expressed from Sf21 insect cells. Analysis by matrix-assisted laser desorption/ionization quadrupole time-of-flight mass spectrometry on the full-length protein sequence of wild-type Sept2 revealed a unique phosphorylation site at residue Ser248 in vivo, which is consistent with one of the twelve phosphorylation sites in the protein sequence theoretically predicted by the Netphos program. Additional predictions with the motif scan programs Scansite and Prosite suggest that the phosphorylation of wild-type Sept2 might be a potential substrate for casein kinase 2. Site-directed mutagenesis of residue 248 from serine to alanine abrogated this phosphorylation. The location of phosphorylation in Sept2 differs from the sites predicted for cGMP-dependent protein kinase (PKG) phosphorylation in Septin 3, raising the possibility that different septins may undergo distinct phosphorylation events that could control their functions in important cellular processes such as neurotransmission or cytokinesis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0951-4198
pubmed:author
pubmed:copyrightInfo
Copyright 2004 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
18
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1123-30
pubmed:dateRevised
2010-10-27
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Septin 2 phosphorylation: theoretical and mass spectrometric evidence for the existence of a single phosphorylation site in vivo.
pubmed:affiliation
Program in Structural Biology and Biochemistry, Hospital for Sick Children, Toronto, Ontario M5G 1X8, Canada. yimin.she@utoronto.ca
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't