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Peter J. Novick, Ph.D.

Professor of Cell Biology
Director of Graduate Admissions

Novick lab website
Phone: (203) 785-5871
Lab: (203) 785-5873/-4316
Fax: (203) 785-7446
e-mail: peter.novick@yale.edu

Department of Cell Biology
Yale University School of Medicine
333 Cedar Street
PO Box 208002
New Haven, CT 06520-8002

<Courier Address>
333 Cedar Street, SHM C-212b/232
New Haven, CT 06510-3206




Our main interest is in membrane traffic as it relates to issues of cell polarity. We are focusing on the final stage of the yeast secretory pathway. Key questions are: How are vesicles transported through the cytoplasm in a vectorial fashion to sites of surface growth? How do vesicles recognize the appropriate target membrane? How does the vesicle membrane fuse with the target membrane?

Vesicle Delivery  Vesicles are transported in a polarized fashion along actin cables by a type V myosin motor under regulation by a GTP binding protein of the rab family, Sec4p and its nucleotide exchange factor, Sec2p. We are studying the regulation of the localization and activity of Sec2p as well as the functional connection between Sec4p and the myosin.

The Exocyst    Secretory vesicles are recognized by an octameric complex, termed the exocyst, which resides at specific sites on the plasma membrane. We are studying the interaction of the exocyst with components of the cell polarity establishment machinery and the mechanism of vesicle-exocyst recognition.

Fusion    Following vesicle recognition, a SNARE complex, involving integral membrane proteins on both the vesicle and plasma membrane, is formed, catalyzing membrane fusion. We are addressing the mechanism of SNARE complex assembly and function, probing roles for the exocyst and a SNARE-binding protein, Sec1p.

ER Inheritance    In collaboration with the Ferro-Novick lab we have initiated a study of ER inheritance in yeast. We are systematically screening the complete library of yeast gene deletions for mutants defective in inheritance of cortical ER. It is already clear that a very similar approach is used to direct the ER into daughter cells as is used in vesicle traffic. Here a different type V myosin, Myo4p, moves the ER into the daughter cell where it is captured by the exocyst complex.

 

Selected Recent Publications
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Elkind NB, Walch-Solimena C, Novick P. (2000)  The role of the COOH terminus of Sec2p in the transport of post-Golgi vesicles.  J Cell. Biol. 149: 95-110.  

Grote E, Carr C, Novick P. (2000)  Ordering the final events in yeast exocytosis.  J Cell Biol. 151: 439-451.  

Grote E, Baba M, Ohsumi Y, Novick P. (2000)  Geranygeranylated SNAREs are dominant inhibitors of membrane fusion.  J Cell Biol. 151: 453-465.  

Guo W, Tamanoi F, Novick P. (2001)  Spatial regulation of the exocyst complex by the Rho1 GTPase.  Nature Cell Biol. 3(4): 353-360.  

Ortiz D, Medkova M, Walch-Solimena C, Novick P. (2002)  Ypt32 recruits the Sec4p guanine nucleotide exchange factor, Sec2p, to secretory vesicles; evidence for a Rab cascade in yeast.  J Cell Biol. 157: 1005-1015.  

Wiederkehr A, Du Y, Pypaert M, Ferro-Novick S, Novick P. (2003)  Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum.  Mol Biol Cell. 14(12): 4770-4782.  






Peter J. Novick