Hook proteins are cytosolic coiled-coil proteins that contain conserved N-terminal domains, which attach to microtubules, and more divergent C-terminal domains, which mediate binding to organelles. The Drosophila Hook protein is a component of the endocytic compartment.[supplied by OMIM
Immunogen
HOOK3 (NP_115786.1, 622 a.a. ~ 718 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
In Caenorhabditis elegans, the HOOK3 (hook microtubule-tethering protein 3) protein is required for connecting the centrosome and the nucleus. It participates in transport of pericentriolar satellites, needed for centrosomal assembly in neurogenesis. HOOK3-RET (ret proto-oncogene) fusion protein is identified in papillary thyroid carcinoma and it results in tumor formation in nude mice. In presence of Salmonella enterica infection, the Salmonella SpiC (pathogenicity island 2 secreted effector protein) inactivates HOOK3 function and thereby affects the cellular trafficking and phagosome-lysosome fusion.
The Salmonella SpiC protein is secreted into the cytosol of macrophages via a unique type III secretion system that functions intracellularly to translocate proteins across the phagosomal membrane. The SpiC protein is required for survival within macrophages and inhibition of
Centrosome functions are important in multiple brain developmental processes. Proper functioning of the centrosome relies on assembly of protein components into the pericentriolar material. This dynamic assembly is mediated by the trafficking of pericentriolar satellites, which are comprised of centrosomal
Chromosomal rearrangements of the RET proto-oncogene (RET/PTC) are the common feature of papillary thyroid carcinoma (PTC). In this study, we report the identification, cloning, and functional characterization of a novel type of RET/PTC rearrangement that results from the fusion of
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