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Sean Conner, Ph.D.

Assistant Professor


Mailing Address:
University of Minnesota
Department of Genetics, Cell Biology, and Development
6-160 Jackson
321 Church St. SE
Minneapolis, MN 55455
USA


Education:
Ph.D. Brown University, 1999

Office:
4-116 MCB
P:612-625-3707
F: 612-625-4648

Email:
sdconner@umn.edu

Webpage:
http://connerlab.dyndns.org/

Lab:
4-180 MCB
P:612-625-4676

Areas of Research Strength:

clathin-mediated endocytic pathway
mammalian vesicular trafficking

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Research Techniques:

adenovirus- and baculovirus-mediated expression
kinase biochemistry
molecular and cell biology

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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.

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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

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