Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

SH2 domain structure and function

B Schaffhausen1

  • 1Department of Biochemistry, Tufts University School of Medicine, Boston, Massachusetts 02111, USA.

Biochimica Et Biophysica Acta
|July 28, 1995
PubMed
Summary

Src homology 2 (SH2) domains are key protein modules that bind tyrosine phosphorylated sequences, regulating signal transduction. Integrating genetic, biochemical, and biophysical data reveals their crucial role in cellular processes.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Inhibition of cell migration by PITENINs: the role of ARF6.

Oncogene·2011
Same author

NMR structure of the N-SH2 of the p85 subunit of phosphoinositide 3-kinase complexed to a doubly phosphorylated peptide reveals a second phosphotyrosine binding site.

Biochemistry·2000
Same author

J domain-independent regulation of the Rb family by polyomavirus large T antigen.

Journal of virology·2000
Same author

Transformation-defective polyoma middle T antigen mutants defective in PLCgamma, PI-3, or src kinase activation enhance ERK2 activation and promote retinoic acid-induced, cell differentiation like wild-type middle T.

Experimental cell research·1999
Same author

Signaling from polyomavirus middle T and small T defines different roles for protein phosphatase 2A.

Molecular and cellular biology·1998
Same author

The DnaJ domain of polyomavirus large T antigen is required to regulate Rb family tumor suppressor function.

Journal of virology·1997

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Signaling

Background:

  • Protein domains exhibit modular functions, regulating catalytic activity or interconnecting regulatory proteins.
  • Src homology 2 (SH2) domains are well-studied protein modules identified by homology in src and fps.
  • SH2 domains bind to tyrosine phosphorylated sequences, playing a critical role in tyrosine kinase regulation.

Purpose of the Study:

  • To explore the integrated understanding of SH2 domains using genetic, biochemical, and biophysical approaches.
  • To highlight the significance of SH2 domains in signal transduction pathways.
  • To demonstrate how diverse experimental results can be synthesized to elucidate protein function.

Main Methods:

  • Review of existing genetic, biochemical, and biophysical studies on SH2 domains.
  • Analysis of SH2 domain interactions with tyrosine phosphorylated sequences.
  • Examination of SH2 domain roles in cellular signaling networks, exemplified by the PDGF receptor.

Main Results:

  • SH2 domains act as crucial mediators in signal transduction by responding to tyrosine phosphorylation.
  • These domains form a regulatable circuitry for timely signal transmission.
  • A common mechanism allows signal generators to coordinate multiple protein targets, such as the PDGF receptor interacting with numerous SH2 domain-containing proteins.

Conclusions:

  • SH2 domains are essential molecular switches in cellular signaling.
  • The integration of multiple research disciplines provides a comprehensive understanding of SH2 domain function.
  • SH2 domains are central to the precise regulation of cellular processes by tyrosine kinases.

Related Experiment Videos