Anti-EHD2 monoclonal antibody, clone FQS0931

The plasma membrane is a dynamic lipid bilayer that engages with the extracellular microenvironment and intracellular cytoskeleton. Caveolae are distinct plasma membrane invaginations lined by integral membrane proteins Caveolin1, 2, and 3. Caveolae formation and stability is further supported by additional proteins including Cavin1, EHD2, Pacsin2 and ROR1. The lipid composition of caveolar membranes, rich in cholesterol and phosphatidylserine, actively contributes to caveolae formation and function. Post-translational modifications of Cav1, including its phosphorylation of the tyrosine-14 residue (pY14Cav1) are vital to its function in and out of caveolae. Cells that experience significant mechanical stress are seen to have abundant caveolae. They play a vital role in regulating cellular signaling and endocytosis, which could further affect the abundance and distribution of caveolae at the PM, contributing to sensing and/or buffering mechanical stress. Changes in membrane tension in cells responding to multiple mechanical stimuli affects the organization and function of caveolae. These mechanical cues regulate pY14Cav1 levels and function in caveolae and focal adhesions. This review, along with looking at the mechanosensitive nature of caveolae, focuses on the role of pY14Cav1 in regulating cellular mechanotransduction. [GRAPHICS] .

Liquid chromatograph-mass spectrometer (LC/MS) based labeled with isobaric mass tags for relative and absolute quantitation (iTRAQ) analyses were performed to identify differentially expressed proteins from normal and cancerous human colorectal tissues. Around 802 proteins were identified, 68 proteins of which were defined as differentially expressed proteins. Bioinformatics analysis indicated that these differentially expressed proteins correlated with several specific cellular processes and pathways which have relationships with pathological changes of colorectal cancer (CRC). EHD2 were selected to verify its expression patterns and localization using western blotting and immunohistochemistry respectively. LC/MS-based iTRAQ proteomic approach would provide new information about the character of CRC.