Disease relevance of EHD2

• The authors have previously described a 150-kilobase minimal deletion region in gliomas that maps to 19q13.33 and contains 3 novel candidate genes (GLTSCR1, EHD2, and GLTSCR2) [1].

High impact information on EHD2

• In contrast, disruption of EHD2 function was without effect on GLUT4 localization or translocation to the plasma membrane [2].
• Here we identified two novel proteins denoted EH domain protein 2 (EHD2) and EHD2-binding protein 1 (EHBP1) that link clathrin-mediated endocytosis to the actin cytoskeleton [3].
• Thus EHD2 appears to connect endocytosis to the actin cytoskeleton through interactions of its N-terminal domain with membranes and its C-terminal EH domain with the novel EHBP1 protein [3].
• These findings strongly suggest that EHD2 interacts with GLUT4 in rat adipocytes and may play a key role in insulin-induced GLUT4 recruitment to the plasma membrane [4].
• Mutation analysis of the five coding exons of EHD2 in gliomas failed to detect any tumor-specific alterations, thus indicating that EHD2 is an unlikely candidate for the 19q tumor suppressor gene [5].

Anatomical context of EHD2

• EHD2 in rat adipocytes was 85% membrane-associated, including approximately 10% in immunopurified GLUT4 vesicles [4].

Associations of EHD2 with chemical compounds

• EHD2 interacts with the insulin-responsive glucose transporter (GLUT4) in rat adipocytes and may participate in insulin-induced GLUT4 recruitment [4].

Other interactions of EHD2

• High expression of EHD2 or EHBP1 in intact cells mediates extensive actin reorganization [3].
• This association of EHD2 with GLUT4 vesicles occurred in PM and three distinct endosomal fractions and was not significantly affected by cellular insulin treatment [4].

Analytical, diagnostic and therapeutic context of EHD2

• On the basis of MALDI-TOF MS, RT-PCR, gene cloning, protein sequencing, and immunoreactivity data, we identified this protein as EHD2, a member of the EH domain-containing proteins that have been implicated in vesicle trafficking [4].
• In co-immunoprecipitation experiments, however, EHD2 physically interacted with GLUT4 in each of these fractions, and cellular insulin treatment selectively enhanced this interaction in an endosomal fraction thought to contain GLUT4 exocytic vesicles [4].

References