Michael  Stankewich, Ph.D.



Associate Research Scientist in Pathology.


Department of Pathology
Yale University School of Medicine
P.O. Box208023
310 Cedar St., BML150
New Haven, CT 0620-8023

Office:
Lab: (203) 785-2771
Fax:

email: michael.stankewich@yale.edu



Training:
Ph.D. Biochemistry, University of Massachusetts Lowell, Lowell, MA
B.S. Biochemistry, Hofstra University, Hempstead, NY

Expertise:
Spectrin cytoskeleton and membrane transport

Research Interests:
A major player of the neuronal cortical cytoskeleton is spectrin, a large and abundant scaffolding protein. The spectrin gene family is comprised of seven genes encoding two alpha and five beta subunits. To add to the complexity, many pre-mRNA splice variants have been identified. The ascribed function for spectrin is stabilizing membranes and organizing protein and lipid micro domains on both the plasma membrane and intracellular organelles. Not only is spectrin important in maintaining membrane micro domains, but also is likely involved in their targeting and transport. Salient characteristics of the spectrin gene family include: 1) a diverse neuronal compartmentalization, 2) Ca2+ /calmodulin mediated regulation, 3) calpain/caspase mediated proteolysis, and 4) tyrosine phosphorylation and ubiquination. My interest is to better elucidate the roles for such sub cellular compartmentalization and posttranslational modifications of the spectrin cytoskeleton and how spectrin affects receptor targeting, trafficking (exocytosis and endocytosis) and stabilization at pre/postsynaptic membranes.

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Selected Publications:

Riordan M, Sreedharan R, Wang S, Thulin G, Mann A, Stankewich M.C, Van Why S, Kashgarian M, Siegel NJ. HSP70 binding modulates detachment of Na-K-ATPase following energy deprivation in renal epithelial cells. Am J Physiol Renal Physiol. 2005 Jun;288(6):F1236-42. 2005 Feb 8.

A. Siddhanta, A. Radulescu, M.C. Stankewich, J.S. Morrow and D.Shields. Fragmentation of the Golgi Apparatus: A role for bIII spectrin and synthesis of phosphatidylinositol (4,5) bisphosphate. J. Biol Chem.2002.

A.G. Vicencio, O. Eickelberg, M.C. Stankewich, M. Kashgarian, G.G Haddad. Regulation of TGF-b ligand and receptor expression in neonatal rat lungs exposed to chronic hypoxia. J. App. Physiol. 93:1123-1130 May 3 2002.

E.A. Holleran, L.A. Ligon, M. Tokito, M.C. Stankewich, J.S. Morrow, and E.L.F. Holzbaur. bIII spectrin binds to the Arp1 subunit of dynactin. J. Biol. Chem. 276: 36598-36605 Sept. 28 2001.

V. Muresan, M.C. Stankewich, W. Steffen, J.S. Morrow, E.L.F. Holzbaur, and B. J. Schnapp. Dynactin-Dependent, Dynein-Driven Vesicle Transport in the Absence of Membrane Proteins: A Role for Spectrin and Acidic Phospholipids. Molec. Cell 7 (1) 173-183 Jan. 19 2001.

M.C. Stankewich, W.T. Tse, L.L. Peters, Y. ChÌng, K.M. Johns, P.R. Stabach, P. Deverajan, J.S. Morrow, and S.E. Lux. A widely expressed b spectrin associated with Golgi and cytoplasmic vesicles. P. Natl. Acad. Sci. USA 95: (24) 14158-14163 Nov. 24 1998.

K.M. McCartney, I.B. Skare, M.C. Stankewich, R.D. Lynch, and E.E. Schneeberger. Occludin is a functional component of the tight junction. J. Cell. Sci. 109:2287-2298 Part 9 Sep. 1996.

M.C. Stankewich, S.A. Francis, Q. Vu, E.E. Schneeberger, and R.D. Lynch. Alterations in cell cholesterol content modulate calcium-induced tight junction assembly by MDCK cells. Lipids 31: (8) 817-828 Aug. 1996.

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This page was last modified on: 09/19/2008