Identification and characterization of novel ERC-55 interacting proteins: Evidence for the existence of several ERC-55 splicing variants; including the cytosolic ERC-55-C

PROTEOMICS ◽  
2009 ◽  
Vol 9 (23) ◽  
pp. 5267-5287 ◽  
Author(s):  
Maja Ludvigsen ◽  
Christian Jacobsen ◽  
Arvid B. Maunsbach ◽  
Bent Honoré
Keyword(s):  
Interacting Proteins ◽  
Splicing Variants ◽  
Identification And Characterization

Kainate receptor-interacting proteins and membrane trafficking

2006 ◽  
Vol 34 (5) ◽  
pp. 927-930 ◽  
Author(s):  
F. Coussen ◽  
C. Mulle
Keyword(s):  
Membrane Trafficking ◽  
Splice Variants ◽  
Kainate Receptors ◽  
Interacting Proteins ◽  
Tail Region ◽  
Protein Partners ◽  
Great Divergence ◽  
Receptor Interacting Proteins ◽  
Identification And Characterization

Kainate receptors are composed of several subunits and splice variants, but the relevance of this diversity is still not well understood. The subunits and splice variants show great divergence in their C-terminal cytoplasmic tail region, which has been identified as a region of interaction with a number of protein partners. Differential trafficking of kainate receptors to neuronal compartments is likely to rely on interactions with distinct subsets of protein partners. This review summarizes our knowledge of the regulation of trafficking of kainate receptors and focuses on the identification and characterization of functions of interacting partners.

scholarly journals ERAP140, a Conserved Tissue-Specific Nuclear Receptor Coactivator

2002 ◽  
Vol 22 (10) ◽  
pp. 3358-3372 ◽  
Author(s):  
Wenlin Shao ◽  
Shlomit Halachmi ◽  
Myles Brown
Keyword(s):  
Nuclear Receptor ◽  
Target Genes ◽  
Tissue Type ◽  
Interacting Proteins ◽  
Nuclear Receptor Coactivator ◽  
Nuclear Receptor Coactivators ◽  
The Brain ◽  
Identification And Characterization

ABSTRACT We report here the identification and characterization of a novel nuclear receptor coactivator, ERAP140. ERAP140 was isolated in a screen for ERα-interacting proteins using the ERα ligand binding domain as a probe. The ERAP140 protein shares no sequence and has little structural homology with other nuclear receptor cofactors. However, homologues of ERAP140 have been identified in mouse, Drosophila, and Caenorhabditis elegans. The expression of ERAP140 is cell and tissue type specific and is most abundant in the brain, where its expression is restricted to neurons. In addition to interacting with ERα, ERAP140 also binds ERβ, TRβ, PPARγ, and RARα. ERAP140 interacts with ERα via a noncanonical interaction motif. The ERα-ERAP140 association can be competed by coactivator NR boxes, indicating ERAP140 binds ERα on a surface similar to that of other coactivators. ERAP140 can enhance the transcriptional activities of nuclear receptors with which it interacts. In vivo, ERAP140 is recruited by estrogen-bound ERα to the promoter region of endogenous ERα target genes. Furthermore, the E2-induced recruitment of ERAP140 to the promoter follows a cyclic pattern similar to that of other coactivators. Our results suggest that ERAP140 represents a distinct class of nuclear receptor coactivators that mediates receptor signaling in specific target tissues.

scholarly journals Identification and characterization of four splicing variants of ovine POU1F1 gene

Gene ◽  
2006 ◽  
Vol 382 ◽  
pp. 12-19 ◽  
Author(s):  
Estela Bastos ◽  
Sílvia Ávila ◽  
Alfredo Cravador ◽  
Robert Renaville ◽  
Henrique Guedes-Pinto ◽  
...  
Keyword(s):  
Pou1f1 Gene ◽  
Splicing Variants ◽  
Identification And Characterization

scholarly journals Identification and Characterization of a Family of Rab11-interacting Proteins

2001 ◽  
Vol 276 (42) ◽  
pp. 39067-39075 ◽  
Author(s):  
Chadwick M. Hales ◽  
Richard Griner ◽  
Karen C. Hobdy-Henderson ◽  
Matthew C. Dorn ◽  
David Hardy ◽  
...  
Keyword(s):  
Interacting Proteins ◽  
Identification And Characterization
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