World Library  


Add to Book Shelf
Flag as Inappropriate
Email this Book

Plos One : Mertk Interactions with Sh2-domain Proteins in the Retinal Pigment Epithelium, Volume 7

By Karl, Mike, O.

Click here to view

Book Id: WPLBN0003940547
Format Type: PDF eBook :
File Size:
Reproduction Date: 2015

Title: Plos One : Mertk Interactions with Sh2-domain Proteins in the Retinal Pigment Epithelium, Volume 7  
Author: Karl, Mike, O.
Volume: Volume 7
Language: English
Subject: Journals, Science, Medical Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary)
Historic
Publication Date:
Publisher: Plos

Citation

APA MLA Chicago

Karl, M. O. (n.d.). Plos One : Mertk Interactions with Sh2-domain Proteins in the Retinal Pigment Epithelium, Volume 7. Retrieved from http://netlibrary.net/


Description
Description : The receptor tyrosine kinase MERTK plays an essential role in the phagocytic uptake of shed photoreceptor membranes by the retinal pigment epithelium (RPE). A fundamental aspect of signal transduction by receptor tyrosine kinases involves autophosphorylation of tyrosine residues that recruit Src-homology 2 (SH2)-domain proteins to the receptor intracellular domain. The goal of the current study was to evaluate the interactions of human MERTK with SH2-domain proteins present in the RPE. The MERTK intracellular domain was expressed as a 6xHis-fusion protein (6xHis-rMERTK571–999), purified and phosphorylated. Ni2+-NTA pull downs were performed using 6xHis-rMERTK571–999 in incubations with recombinant phosphotyrosine-recognition sequences expressed as GST-fusion proteins. In addition, pull downs of native SH2-domain proteins were performed using 6xHis-rMERTK571–999 and protein homogenates from rat RPE/choroid. For both recombinant and native proteins, western analysis detected MERTK interactions with GRB2, PIK3R1 (P85a), VAV3, and SRC. Immunohistochemical analysis localized each protein to mouse RPE. In cultured RPE-J cells incubated with rod outer segments (OS), siRNA knockdown of Grb2 had no effect on OS binding, but significantly reduced OS uptake. Pik3r1 localized to early phagosomes along with Rab5 and Eea1. Phosphorylation and activation of Src was detected downstream of phagocytosis and Mertk activation. These findings suggest that MERTK signaling in the RPE involves a cohort of SH2-domain proteins with the potential to regulate both cytoskeletal rearrangement and membrane movement. Identification of the SH2-domain signaling partners of MERTK is an important step toward further defining the mechanism of RPE phagocytosis that is central to the function and survival of the retina.

 

Click To View

Additional Books


  • Plos One : Molecular Characterization of... (by )
  • Plos One : Inhibition of P-glycoprotein ... (by )
  • Plos One : Do We Deliver the Pressures W... (by )
  • Plos One : Identification of Genes Invol... (by )
  • Plos One : Epigenetic Differentiation Pe... (by )
  • Plos One : Distribution of Central Corne... (by )
  • Plos One : the Role of Mechanical Force ... (by )
  • Plos One : Apobec3G-augmented Stem Cell ... (by )
  • Plos One : Regulation of the Formyl Pept... (by )
  • Plos One : Genome-wide Association Ident... (by )
  • Plos One : Detecting Semantic Priming at... (by )
  • Plos One : Identification of Proteins fr... (by )
Scroll Left
Scroll Right

 



Copyright © World Library Foundation. All rights reserved. eBooks from World Library are sponsored by the World Library Foundation,
a 501c(4) Member's Support Non-Profit Organization, and is NOT affiliated with any governmental agency or department.