The TRP Ca2+channel assembled in a signaling complex by the PDZ domain protein INAD is phosphorylated through the interaction with protein kinase C (ePKC)-Reference-Cited by-同舟云学术

The TRP Ca2+channel assembled in a signaling complex by the PDZ domain protein INAD is phosphorylated through the interaction with protein kinase C (ePKC)

Published:1998-03-27 Issue:2 Volume:425 Page:317-322
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Huber Armin,Sander Philipp,Bähner Monika,Paulsen Reinhard

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/S0014-5793(98)00248-8/fullpdf

Reference34 articles.

1. Clustering Membrane Proteins: It's All Coming Together with the PSD-95/SAP90 Protein Family

2. The transient receptor potential protein (Trp), a putative store-operated Ca2+ channel essential for phosphoinositide-mediated photoreception, forms a signaling complex with NorpA, InaC and InaD.

3. Requirement for the PDZ Domain Protein, INAD, for Localization of the TRP Store-Operated Channel to a Signaling Complex

4. A multivalent PDZ-domain protein assembles signalling complexes in a G-protein-coupled cascade

5. Novel Ca2+ channels underlying transduction in Drosophila photoreceptors: implications for phosphoinositide-mediated Ca2+ mobilization

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