English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Phosphoproteome of Pristionchus pacificus Provides Insights into Architecture of Signaling Networks in Nematode Models

Borchert, N., Krug, K., Gnad, F., Sinha, A., Sommer, R. J., & Macek, B. (2012). Phosphoproteome of Pristionchus pacificus Provides Insights into Architecture of Signaling Networks in Nematode Models. MOLECULAR & CELLULAR PROTEOMICS, 11(12 Spec. Iss.), 1631-1639. doi:10.1074/mcp.M112.022103.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Borchert, Nadine1, Author
Krug, Karsten1, Author
Gnad, Florian2, Author           
Sinha, Amit1, Author
Sommer, Ralf J.1, Author
Macek, Boris1, Author
Affiliations:
1external, ou_persistent22              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              

Content

show
hide
Free keywords: CAENORHABDITIS-ELEGANS; MASS-SPECTROMETER; TOOL; PHOSPHORYLATION; ANNOTATION; PREDICTION; ACCURACY; PROTEINS; DATABASE; BIOLOGY
 Abstract: Pristionchus pacificus is a nematode that is increasingly used as a model organism in evolutionary biology. The genome of P. pacificus differs markedly from that of C. elegans, with a high number of orphan genes that are restricted to P. pacificus and have no homologs in other species. To gain insight into the architecture of signal transduction networks in model nematodes, we performed a large-scale qualitative phosphoproteome analysis of P. pacificus. Using two-stage enrichment of phosphopeptides from a digest of P. pacificus proteins and their subsequent analysis via high accuracy MS, we detected and localized 6,809 phosphorylation events on 2,508 proteins. We compared the detected P. pacificus phosphoproteome to the recently published phosphoproteome of C. elegans. The overall numbers and functional classes of phosphoproteins were similar between the two organisms. Interestingly, the products of orphan genes were significantly underrepresented among the detected P. pacificus phosphoproteins. We defined the theoretical kinome of P. pacificus and compared it to that of C. elegans. While tyrosine kinases were slightly underrepresented in the kinome of P. pacificus, all major classes of kinases were present in both organisms. Application of our kinome annotation to a recent transcriptomic study of dauer and mixed stage populations showed that Ser/Thr and Tyr kinases show similar expression levels in P. pacificus but not in C. elegans. This study presents the first systematic comparison of phosphoproteomes and kinomes of two model nematodes and, as such, will be a useful resource for comparative studies of their signal transduction networks. Molecular & Cellular Proteomics 11: 10.1074/mcp.M112.022103, 1631-1639, 2012.

Details

show
hide
Language(s): eng - English
 Dates: 2012-12
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000313557000011
DOI: 10.1074/mcp.M112.022103
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: MOLECULAR & CELLULAR PROTEOMICS
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: 9650 ROCKVILLE PIKE, BETHESDA, MD 20814-3996 USA : AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Pages: - Volume / Issue: 11 (12 Spec. Iss.) Sequence Number: - Start / End Page: 1631 - 1639 Identifier: ISSN: 1535-9476