PMID- 24899341
OWN - NLM
STAT- MEDLINE
DCOM- 20150408
LR  - 20220129
IS  - 1535-9484 (Electronic)
IS  - 1535-9476 (Print)
IS  - 1535-9476 (Linking)
VI  - 13
IP  - 8
DP  - 2014 Aug
TI  - Global analysis of muscle-specific kinase signaling by quantitative 
      phosphoproteomics.
PG  - 1993-2003
LID - 10.1074/mcp.M113.036087 [doi]
AB  - The development of the neuromuscular synapse depends on signaling processes that 
      involve protein phosphorylation as a crucial regulatory event. Muscle-specific 
      kinase (MuSK) is the key signaling molecule at the neuromuscular synapse whose 
      activity is required for the formation of a mature and functional synapse. 
      However, the signaling cascade downstream of MuSK and the regulation of the 
      different components are still poorly understood. In this study we used a 
      quantitative phosphoproteomics approach to study the phosphorylation events and 
      their temporal regulation downstream of MuSK. We identified a total of 10,183 
      phosphopeptides, of which 203 were significantly up- or down-regulated. Regulated 
      phosphopeptides were classified into four different clusters according to their 
      temporal profiles. Within these clusters we found an overrepresentation of 
      specific protein classes associated with different cellular functions. In 
      particular, we found an enrichment of regulated phosphoproteins involved in 
      posttranscriptional mechanisms and in cytoskeletal organization. These findings 
      provide novel insights into the complex signaling network downstream of MuSK and 
      form the basis for future mechanistic studies.
CI  - (c) 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
FAU - Durnberger, Gerhard
AU  - Durnberger G
AD  - From the double daggerGregor Mendel Institute of Molecular Plant Biology, Dr. Bohr-Gasse 3, 
      1030 Vienna, Austria;  section signInstitute for Molecular Pathology (IMP), Dr. Bohr-Gasse 7, 
      1030 Vienna, Austria;  paragraph signInstitute of Molecular Biotechnology (IMBA), Dr. 
      Bohr-Gasse 3, 1030 Vienna, Austria;
FAU - Camurdanoglu, Bahar Z
AU  - Camurdanoglu BZ
AD  -  ||Center for Brain Research, Medical University of Vienna, Spitalgasse 4, 1090 
      Vienna, Austria;
FAU - Tomschik, Matthias
AU  - Tomschik M
AD  -  ||Center for Brain Research, Medical University of Vienna, Spitalgasse 4, 1090 
      Vienna, Austria;
FAU - Schutzbier, Michael
AU  - Schutzbier M
AD  - From the double daggerGregor Mendel Institute of Molecular Plant Biology, Dr. Bohr-Gasse 3, 
      1030 Vienna, Austria;  section signInstitute for Molecular Pathology (IMP), Dr. Bohr-Gasse 7, 
      1030 Vienna, Austria;
FAU - Roitinger, Elisabeth
AU  - Roitinger E
AD  -  section signInstitute for Molecular Pathology (IMP), Dr. Bohr-Gasse 7, 1030 Vienna, Austria; 
       paragraph signInstitute of Molecular Biotechnology (IMBA), Dr. Bohr-Gasse 3, 1030 Vienna, 
      Austria;
FAU - Hudecz, Otto
AU  - Hudecz O
AD  -  section signInstitute for Molecular Pathology (IMP), Dr. Bohr-Gasse 7, 1030 Vienna, Austria; 
       paragraph signInstitute of Molecular Biotechnology (IMBA), Dr. Bohr-Gasse 3, 1030 Vienna, 
      Austria;
FAU - Mechtler, Karl
AU  - Mechtler K
AD  -  section signInstitute for Molecular Pathology (IMP), Dr. Bohr-Gasse 7, 1030 Vienna, Austria; 
       paragraph signInstitute of Molecular Biotechnology (IMBA), Dr. Bohr-Gasse 3, 1030 Vienna, 
      Austria;
FAU - Herbst, Ruth
AU  - Herbst R
AD  -  ||Center for Brain Research, Medical University of Vienna, Spitalgasse 4, 1090 
      Vienna, Austria; double daggerdouble daggerInstitute of Immunology, Medical University of Vienna, 
      Lazarettgasse 19, 1090 Vienna, Austria.
LA  - eng
GR  - P 24685/FWF_/Austrian Science Fund FWF/Austria
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20140604
PL  - United States
TA  - Mol Cell Proteomics
JT  - Molecular & cellular proteomics : MCP
JID - 101125647
RN  - 0 (Agrin)
RN  - 0 (Phosphopeptides)
RN  - EC 2.7.10.1 (MuSK protein, mouse)
RN  - EC 2.7.10.1 (Receptor Protein-Tyrosine Kinases)
SB  - IM
MH  - Agrin/pharmacology
MH  - Animals
MH  - Cell Line
MH  - Cytoskeleton/metabolism
MH  - Gene Expression Regulation
MH  - Mice
MH  - Muscle, Skeletal/*metabolism
MH  - Phosphopeptides/*isolation & purification/metabolism
MH  - Proteomics/*methods
MH  - RNA Processing, Post-Transcriptional
MH  - Receptor Protein-Tyrosine Kinases/*metabolism
MH  - Signal Transduction
PMC - PMC4125732
EDAT- 2014/06/06 06:00
MHDA- 2015/04/09 06:00
PMCR- 2015/08/01
CRDT- 2014/06/06 06:00
PHST- 2014/06/06 06:00 [entrez]
PHST- 2014/06/06 06:00 [pubmed]
PHST- 2015/04/09 06:00 [medline]
PHST- 2015/08/01 00:00 [pmc-release]
AID - S1535-9476(20)34882-9 [pii]
AID - M113.036087 [pii]
AID - 10.1074/mcp.M113.036087 [doi]
PST - ppublish
SO  - Mol Cell Proteomics. 2014 Aug;13(8):1993-2003. doi: 10.1074/mcp.M113.036087. Epub 
      2014 Jun 4.