PMID- 10210201
OWN - NLM
STAT- MEDLINE
DCOM- 19990714
LR  - 20181113
IS  - 0961-8368 (Print)
IS  - 0961-8368 (Linking)
VI  - 8
IP  - 1
DP  - 1999 Jan
TI  - Identification of Tyr438 as the major in vitro c-Src phosphorylation site in
      human gelsolin: a mass spectrometric approach.
PG  - 234-41
AB  - Gelsolin is an actin-binding protein (82 kDa) consisting of six repeated segments
      (S1-S6), each approximately 120 residues long. It interacts with phospholipids
      and we previously showed that phosphatidylinositol 4,5-bisphosphate promotes
      phosphorylation of gelsolin by the tyrosine kinase c-Src. We used a combination
      of different methods, such as thin-layer chromatography and
      anti-phosphotyrosine-agarose immunoprecipitation of phosphopeptides combined with
      matrix assisted laser desorption ionization-mass spectrometry (MALDI-MS) and post
      source decay (PSD) analysis, to identify the phosphorylation sites in gelsolin.
      The major phosphorylation site (Tyr438) was located in subdomain 4 (S4).
      Phosphorylation of gelsolin in the gelsolin-actin2 complex was inhibited by 90%. 
      Gelsolin phosphorylation by c-Src in the presence of lysophosphatidic acid also
      revealed Tyr438 as the most prominent site. Additional minor sites were found
      using the anti-phosphotyrosine bead immunoprecipitation method followed by
      MALDI-MS and PSD analysis. These sites, representing approximately 5% of the
      total phosphate incorporation, were identified as Tyr59, Tyr382, Tyr576, and
      Tyr624. Based on these results we generated antibodies which specifically
      recognize Tyr438 phosphorylated gelsolin.
FAU - De Corte, V
AU  - De Corte V
AD  - Flanders Interuniversity Institute for Biotechnology, Department of Biochemistry,
      Faculty of Medicine, Universiteit Gent, Ghent, Belgium.
FAU - Demol, H
AU  - Demol H
FAU - Goethals, M
AU  - Goethals M
FAU - Van Damme, J
AU  - Van Damme J
FAU - Gettemans, J
AU  - Gettemans J
FAU - Vandekerckhove, J
AU  - Vandekerckhove J
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Protein Sci
JT  - Protein science : a publication of the Protein Society
JID - 9211750
RN  - 0 (Actins)
RN  - 0 (Gelsolin)
RN  - 0 (Lysophospholipids)
RN  - 0 (Phosphatidylinositol 4,5-Diphosphate)
RN  - 42HK56048U (Tyrosine)
RN  - EC 2.7.10.2 (Proto-Oncogene Proteins pp60(c-src))
SB  - IM
MH  - Actins/chemistry
MH  - Amino Acid Sequence
MH  - Dimerization
MH  - Gelsolin/chemistry/*metabolism
MH  - Humans
MH  - Lysophospholipids/chemistry
MH  - Molecular Sequence Data
MH  - Peptide Mapping
MH  - Phosphatidylinositol 4,5-Diphosphate/chemistry
MH  - Phosphorylation
MH  - Proto-Oncogene Proteins pp60(c-src)/*metabolism
MH  - Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
MH  - Tyrosine/*metabolism
PMC - PMC2144107
EDAT- 1999/04/21 00:00
MHDA- 1999/04/21 00:01
CRDT- 1999/04/21 00:00
PHST- 1999/04/21 00:00 [pubmed]
PHST- 1999/04/21 00:01 [medline]
PHST- 1999/04/21 00:00 [entrez]
AID - 10.1110/ps.8.1.234 [doi]
PST - ppublish
SO  - Protein Sci. 1999 Jan;8(1):234-41. doi: 10.1110/ps.8.1.234.