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Return to: College of Biological Sciences: Medical School: U of M Home |
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Areas of Research Strength: clathin-mediated endocytic pathway mammalian vesicular trafficking back to top |
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Research Techniques: adenovirus- and baculovirus-mediated expression kinase biochemistry molecular and cell biology back to top |
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Research Interests: Clathrin-mediated endocytosis is fundamental to a diverse range of biological processes. For example, clathrin-coated vesicles mediate the clearance of receptor-bound hormones and growth factors from the plasma membrane, are important for nutrient uptake, and are vital to the recycling of synaptic vesicles in neurons. While more than 30 proteins are thought to be involved in this ubiquitous internalization pathway, two oligomeric protein complexes, clathrin and AP2, constitute the major coat proteins of these vesicles. Accumulating evidence suggests that coat protein phosphorylation is a key step in the spatial and temporal regulation of the clathrin-mediated endocytic pathway. For example, treatment of cells with kinase or phosphatase inhibitors that disrupt coat protein (de)phosphorylation severely disrupts endocytosis. Our research focuses on determining the impact of phosphorylation on coat protein function by: 1) isolating and characterizing kinases that specifically target endocytic machinery, and 2) defining the functional consequence of phosphorylation on coat protein assembly and recruitment to biological membranes using mammalian in vitro assays that reconstitute various steps of the internalization process. back to top |
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Selected Publications: Conner SD and Schmit SL (2005) CVAK104 is a novel poly-L-lysine stimulated kinase that targets the B2 subunit of AP2 J. Biol. Chem 280:21539-44. Conner, S.D., Schröter, T., and Schmid, S.L. (2003) AAK1-mediated µ2 phospohrylation is stimulated by assembled clathrin Traffic. 4:885-90 Conner, S.D., and Schmid, S.L. (2003) Regulated Portals of Entry into the Cell. Nature. 422:37-44 Conner, S.D. and Schmid, S.L. (2003) Differential Requirements for AP2 in Clathrin-Mediated Endocytosis. J. Cell Biol. 162:773-79 Conner S.D. and Schmid, S.L. (2002) Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis. J Cell Biol. 156:921-9. Ricotta D, Conner S.D., Schmid S.L., von Figura K, Honing S. (2002) Phosphorylation of the AP2 µ subunit by AAK1 mediates high affinity binding to membrane protein sorting signals. J Cell Biol. 156:791-5. To view these and other publications visit http://www.ncbi.nlm.nih.gov/PubMed search menu should say PubMed type Conner SD in the avaliable line back to top |
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