English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Cutting edge: Feed-forward activation of phospholipase C gamma 2 via C2 domain-mediated binding to SLP65.

Engelke, M., Oellerich, T., Dittmann, K., Hsiao, H. H., Urlaub, H., Serve, H., et al. (2013). Cutting edge: Feed-forward activation of phospholipase C gamma 2 via C2 domain-mediated binding to SLP65. Journal of Immunology, 191(11), 5354-5358. doi:10.4049/jimmunol.1301326.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-CE0D-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CB51-7
Genre: Journal Article

Files

show Files
hide Files
:
1877922.pdf (Publisher version), 2MB
 
File Permalink:
-
Name:
1877922.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Biophysical Chemistry (Karl Friedrich Bonhoeffer Institute), Göttingen; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-
:
1877922_Suppl_1.pdf (Supplementary material), 2MB
Name:
1877922_Suppl_1.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Engelke, M., Author
Oellerich, T., Author
Dittmann, K., Author
Hsiao, H. H.1, Author              
Urlaub, H.1, Author              
Serve, H., Author
Griesinger, C.2, Author              
Wienands, J., Author
Affiliations:
1Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: -
 Abstract: Ag-mediated B cell stimulation relies on phospholipase C gamma 2 (PLC gamma 2) for Ca2+ mobilization. Enzymatic activity of PLC gamma 2 is triggered upon Src homology 2 domain-mediated binding to the tyrosine-phosphorylated adaptor SLP65. However, SLP65 phosphorylation outlasts the elevation of cytosolic Ca2+ concentration suggesting additional levels of PLC gamma 2 regulation. We show in this article that the functionality of the PLC gamma 2/SLP65 complex is controlled by the weakly characterized C2 domain of PLC gamma 2. Usually C2 domains bind membrane lipids, but that of PLC gamma 2 docks in a Ca2+-regulated manner to a distinct phosphotyrosine of SLP65. Hence, early Ca2+ fluxing provides feed-forward signal amplification by promoting anchoring of the PLC gamma 2 C2 domain to phospho-SLP65. As the cellular Ca2+ resources become exhausted, the concomitant decline of Ca2+ dampens the C2-phosphotyrosine interaction so that PLC gamma 2 activation terminates despite sustained SLP65 phosphorylation.

Details

show
hide
Language(s): eng - English
 Dates: 2013-10-282013-12-01
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.4049/jimmunol.1301326
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Journal of Immunology
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 191 (11) Sequence Number: - Start / End Page: 5354 - 5358 Identifier: -