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BAG proteins compete with Hip for binding to the Hsc70/Hsp70 ATPase domain and promote substrate release. All the BAG proteins have an approximately 45-amino acid BAG domain near the C terminus but differ markedly in their N-terminal regions. The predicted BAG2 protein contains 211 amino acids. The BAG domains of BAG1, BAG2, and BAG3 interact specifically with the Hsc70 ATPase domain in vitro and in mammalian cells. All 3 proteins bind with high affinity to the ATPase domain of Hsc70 and in

May play a role in mediating neutrophil activation and chemotaxis.

Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses. Multiple alternatively spliced transcript variants encoding different isofor

The distinct peripheral cytosolic proteins, alpha, beta and gamma-catenin (102, 94 and 86 kDa) found in many tissues bind to the conserved cytoplasmic tail domain of the cell-adhesion cadherins. Catenins link E-cadherin to other integral membrane or cytoplasmic proteins and are modulated by Wnt-1 proto-oncogene. They are good candidates for mediating transduction of cell-cell contact positional signals to the cell interior. Absence of alpha-catenin is found in certain tumor cell lines and r