Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
 
Articles by S Snyder
Total Records ( 1 ) for S Snyder
  L Rider , J Tao , S Snyder , B Brinley , J Lu and M. Diakonova
 

The Src homology 2 (SH2) domain-containing adapter protein SH2B1β plays a role in severe obesity, leptin and insulin resistance, and infertility. SH2B1β was initially identified as a Janus tyrosine kinase 2 (JAK2) substrate, and it has been implicated in cell motility and regulation of the actin rearrangement in response to GH and platelet-derived growth factor. SH2B1β is also required for maximal actin-based motility of Listeria. Here we have used a low-speed pelleting assay and electron microscopy to demonstrate that SH2B1β has two actin-binding sites and that it cross-links actin filaments in vitro. Wild-type SH2B1β localized to cell ruffles and along filopodia, but deletion of amino acids 150–200 (the first actin-binding site) led to mislocalization of the protein to filopodia tip complexes where it colocalized with vasodilator-stimulated phosphoprotein (VASP). Based on studies performed in VASP-deficient MVD7–/– cells, with or without green fluorescent protein-VASP reconstitution, we concluded that the proper intracellular localization of native SH2B1β required the presence of the first SH2B1β actin-binding site and VASP. Finally, we found that both SH2B1β actin-binding domains were required for maximal GH- and prolactin-induced cell ruffling. Together, these results suggest that SH2B1β functions as an adapter protein that cross-links actin filaments, leading to modulation of cellular responses in response to JAK2 activation.

 
 
 
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility