Proteomics

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Systems-wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation

ABSTRACT: In this study, we have analyzed BCR induced dynamic composition of the BCR signalosome and global changes in BCR induced phosphoproteome and ubiquitylation events using high resolution LC-MS/MS

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): B Cell

SUBMITTER: Shankha Satpathy  

LAB HEAD: Chunaram Choudhary

PROVIDER: PXD001440 | Pride | 2015-06-02

REPOSITORIES: Pride

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20120521_QE4_LC6_SAW_SA_A20_SILAC_IgG_RepA_GG_SCX_01.raw Raw
20120521_QE4_LC6_SAW_SA_A20_SILAC_IgG_RepA_GG_SCX_02.raw Raw
20120521_QE4_LC6_SAW_SA_A20_SILAC_IgG_RepA_GG_SCX_03.raw Raw
20120521_QE4_LC6_SAW_SA_A20_SILAC_IgG_RepA_GG_SCX_04.raw Raw
20120521_QE4_LC6_SAW_SA_A20_SILAC_IgG_RepA_GG_SCX_05.raw Raw
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Publications

Systems-wide analysis of BCR signalosomes and downstream phosphorylation and ubiquitylation.

Satpathy Shankha S   Wagner Sebastian A SA   Beli Petra P   Gupta Rajat R   Kristiansen Trine A TA   Malinova Dessislava D   Francavilla Chiara C   Tolar Pavel P   Bishop Gail A GA   Hostager Bruce S BS   Choudhary Chunaram C  

Molecular systems biology 20150602 6

B-cell receptor (BCR) signaling is essential for the development and function of B cells; however, the spectrum of proteins involved in BCR signaling is not fully known. Here we used quantitative mass spectrometry-based proteomics to monitor the dynamics of BCR signaling complexes (signalosomes) and to investigate the dynamics of downstream phosphorylation and ubiquitylation signaling. We identify most of the previously known components of BCR signaling, as well as many proteins that have not ye  ...[more]