The cell migration molecule UNC-53/NAV2 interacts with C. elegans verprolin and Abelson kinase interactor. Export

@inproceedings{citeulike:3321885, abstract = {UNC-53/NAV2 is required for the guidance and extension of a subset of cells in C.elegans, including the sex muscles, several axons and the excretory canals. UNC-53 protein binds F-actin, and the SH2SH3 adapter protein SEM-5/GRB2 in vitro, implicating UNC-53 in both signal transduction and actin cytoskeleton dynamics (Stringham et al., 2002, Development 129:3367-3379). While UNC-53 clearly has a role in the guidance of the developing nervous system we have shown it is also expressed in adult cells. Anti-UNC53 antiserum stains the excretory canals, coelomocytes and neurons suggesting that UNC-53 is also required after completion of outgrowth. Through proteomics we have identified two molecules that interact with UNC-53 at its N-terminus; B0336.6, the C. elegans homologue to ABI (Abelson tyrosine kinase interactor), and T12G3.1, the homologue to yeast verprolin. The yeast protein interaction database identified verprolin and Ysc84p/ABI as interactors with Sla1p, a multifunctional protein that couples the yeast endocytic machinery to proteins regulating actin dynamics. These data suggest that UNC-53, together with verprolin, ABI and Sla1p may form a complex at the cytoskeleton that stabilizes or promotes actin polymerization. Moreover, we have observed expression of UNC-53 protein in the coelomocytes, which are phagocytic cells suggesting a possible role for UNC-53/NAV2 in endocytic pathways. We are currently testing this hypothesis using a transgenic reporter that produces a secretable form of GFP (Fares et al., 2001, Genetics 159:133-145). Co-localization studies of UNC-53/NAV2 with T12G3.1::gfp show that both proteins are expressed in certain neurons and the vulval muscles. Interestingly, while UNC-53 is expressed in the excretory cell T12G3.1/verprolin is not, but it is expressed in the excretory gland, a secretory cell. The RNAi phenotype of C. elegans B0336.6 is embryonic lethal. We are currently raising antibodies against the B0336.6 gene product in order to determine its pattern of expression in C. elegans. (Supported by a Discovery grant from the Natural Sciences and Engineering Research Council of Canada to E.S.).}, author = {Schmidt, Kristopher L. and Marcus, Nancy and Baillie, David and Stringham, Eve G.}, citeulike-article-id = {3321885}, citeulike-linkout-0 = {http://www.wormbase.org/db/misc/paper?name=WBPaper00026285}, journal = {International Worm Meeting}, keywords = {abi-1, b03366, c\_elegans, caenorhabditis\_elegans, celegans, elegans, meeting\_abstract, nematode, wormbase}, posted-at = {2008-09-23 15:00:41}, priority = {3}, title = {The cell migration molecule UNC-53/NAV2 interacts with C. elegans verprolin and Abelson kinase interactor.}, url = {http://www.wormbase.org/db/misc/paper?name=WBPaper00026285}, year = {2005} }

TY - CONF ID - citeulike:3321885 L3 - citeulike-article-id:3321885 N2 - UNC-53/NAV2 is required for the guidance and extension of a subset of cells in C.elegans, including the sex muscles, several axons and the excretory canals. UNC-53 protein binds F-actin, and the SH2SH3 adapter protein SEM-5/GRB2 in vitro, implicating UNC-53 in both signal transduction and actin cytoskeleton dynamics (Stringham et al., 2002, Development 129:3367-3379). While UNC-53 clearly has a role in the guidance of the developing nervous system we have shown it is also expressed in adult cells. Anti-UNC53 antiserum stains the excretory canals, coelomocytes and neurons suggesting that UNC-53 is also required after completion of outgrowth. Through proteomics we have identified two molecules that interact with UNC-53 at its N-terminus; B0336.6, the C. elegans homologue to ABI (Abelson tyrosine kinase interactor), and T12G3.1, the homologue to yeast verprolin. The yeast protein interaction database identified verprolin and Ysc84p/ABI as interactors with Sla1p, a multifunctional protein that couples the yeast endocytic machinery to proteins regulating actin dynamics. These data suggest that UNC-53, together with verprolin, ABI and Sla1p may form a complex at the cytoskeleton that stabilizes or promotes actin polymerization. Moreover, we have observed expression of UNC-53 protein in the coelomocytes, which are phagocytic cells suggesting a possible role for UNC-53/NAV2 in endocytic pathways. We are currently testing this hypothesis using a transgenic reporter that produces a secretable form of GFP (Fares et al., 2001, Genetics 159:133-145). Co-localization studies of UNC-53/NAV2 with T12G3.1::gfp show that both proteins are expressed in certain neurons and the vulval muscles. Interestingly, while UNC-53 is expressed in the excretory cell T12G3.1/verprolin is not, but it is expressed in the excretory gland, a secretory cell. The RNAi phenotype of C. elegans B0336.6 is embryonic lethal. We are currently raising antibodies against the B0336.6 gene product in order to determine its pattern of expression in C. elegans. (Supported by a Discovery grant from the Natural Sciences and Engineering Research Council of Canada to E.S.). JF - International Worm Meeting TI - The cell migration molecule UNC-53/NAV2 interacts with C. elegans verprolin and Abelson kinase interactor. KW - abi-1 KW - b03366 KW - c_elegans KW - caenorhabditis_elegans KW - celegans KW - elegans KW - meeting_abstract KW - nematode KW - wormbase AU - Schmidt, Kristopher AU - Marcus, Nancy AU - Baillie, David AU - Stringham, Eve PY - 2005/// UR - http://www.wormbase.org/db/misc/paper?name=WBPaper00026285 ER -