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

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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

Novick, P. and R. Schekman, 1979.  Secretion and cell surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae.  Proc. Natl. Acad. Sci. USA 76: 1858-1862.

Novick, P., C. Field and R. Schekman, 1980.  Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway.  Cell 21: 205-215.

Esmon, B., P. Novick and R. Schekman, 1981.  Compartmentalized assembly of oligosaccharides on exported glycoproteins in yeast.  Cell 25: 451-460.

Novick, P., S. Ferro and R. Schekman, 1981.  Order of events in the yeast secretory pathway.  Cell 25: 461-469.

Schekman, R. and P. Novick, 1982.  The secretory process and yeast cell surface assembly.  In:  Molecular Biology of the Yeast Saccharomyces, Vol. 2 (J. Strathern et al., eds.), Cold Spring Harbor Laboratory.

Schekman, R., P. Novick, S. Ferro-Novick, B. Esmon, W. Hansen, T. Etcheverry and T. Stevens, 1982.  Secretion and organelle assembly in yeast.  Berkeley Workshop on Recent Advances in Yeast Molecular Biology 1: 143.

Novick, P. and R. Schekman, 1983.  Export of major cell surface proteins is blocked in yeast secretory mutants.  J. Cell Biol. 96: 541-547.

Schekman, R., B. Esmon, S. Ferro, C. Field and P. Novick, 1983.  Yeast secretory mutants:  Isolation and characterization.  Methods in Enzymology 96: 802-815.

Ferro-Novick, S., P. Novick, C. Field and R. Schekman, 1984.  Yeast secretory mutants that block the formation of active surface enzymes.  J. Cell Biol. 98: 35-43.

Thomas, J., P. Novick and D. Botstein, 1984.  Genetics of the yeast cytoskeleton.  In:  Molecular Biology of the Cytoskeleton (G. Borisy, D. Cleveland and D. Murphy, eds.), Cold Spring Harbor Laboratory, Cold Spring Harbor, New York.

Novick, P., J. Thomas and D. Botstein, 1984.  Genetic analysis of cytoskeletal protein function in yeast.  In:  Genetic Engineering, Vol. 6 (J. Setlow and A. Hollaender, eds.), Plenum Press.

Shortle, D., P. Novick and D. Botstein, 1984.  Construction and genetic characterization of temperature-sensitive mutant alleles of the yeast actin gene.  Proc. Natl. Acad. Sci. USA 81: 4889-4893.

Novick, P. and D. Botstein, 1985. Phenotypic analysis of temperature-sensitive yeast actin mutants.  Cell 40: 405-416.

Novick, P., 1985.  Intracellular transport mutants of yeast.  TIBS 10: 432-434.

Salminen, A. and P. Novick, 1987.  A ras-like protein is required for a post-Golgi event in yeast secretion.  Cell 49: 527-538.

Walworth, N.C. and P. Novick, 1987.  Isolation and characterization of constitutive secretory vesicles from a yeast secretory mutant.  J. Cell Biol. 105: 163-174.

Rose, M., P. Novick, J. Thomas, D. Botstein and G. Fink, 1987.  A Saccharomyces cerevisae genomic plasmid bank based on a centromere containing shuttle vector.  Gene 60: 237-243.

Goud, B., A. Salminen, N.C. Walworth and P. Novick, 1988.  A GTP-binding protein required for secretion rapidly associates with secretory vesicles and the plasma membrane in yeast.  Cell 53: 753-768.

Novick, P., B. Goud, A. Salminen, N.C. Walworth, J. Nair and M. Potenza, 1988. Regulation of vesicular traffic by a GTP-binding protein on the cytoplasmic surface of secretory vesicles in yeast.  Cold Spring Harbor Symposium on Quantitative Biology, 53: 637-647.

Walworth, N.C., B. Goud, H. Ruohola and P. Novick, 1989.  Fractionation of yeast organelles.  Methods in Cell Biology 31: 335-354.

Novick, P., B.C. Osmond and D. Botstein, 1989.  Suppressors of yeast actin mutations.  Genetics, 121: 659-674.

Walworth, N.C., B. Goud, A.K. Kabcenell and P. Novick, 1989.  Mutational analysis of SEC4 suggests a cyclical mechanism for the regulation of vesicular traffic.  EMBO J., 8: 1685-1993.

Bacon, R. A.,  A. Salminen, H. Ruohola, P. Novick and S. Ferro-Novick. 1989. The GTP binding protein, Ypt1, is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants. J. Cell Biol. 109: 1015-1022. 

Salminen, A. and P. Novick, 1989. The Sec15 protein responds to the function of the GTP binding protein, Sec4, to control vesicular traffic. J. Cell Biol. 109: 1023-1036.

Cleves, A. E., P. Novick and V. A. Bankaitis. 1989. Mutations in the SAC1 gene suppress defects in the yeast Golgi and yeast actin function. J. Cell Biol. 109: 2939-2950.

Nair, J., H. Müller, M. Peterson and P. Novick. 1990. Sec2 protein contains a coiled-coil domain essential for vesicular transport and a dispensable carboxy terminal domain. J. Cell Biol. 110: 1897-1909.

Kabcenell, A. K., B. Goud, J. K. Northup and P. Novick. 1990. Binding and hydrolysis of guanine nucleotides by Sec4p, a yeast protein involved in the regulation of vesicular traffic. J. Biol. Chem. 265: 9366-9372.

Bowser, R. and P. Novick. 1991. Sec15 protein, an essential component of the exocytotic apparatus, is associated with the plasma membrane and with a soluble 19.5S particle. J. Cell Biol. 112: 1117-1131.

Sasaki ,T., K. Kaibuchi, A.K. Kabcenell, P. Novick, and Y. Takai. 1991. A mammalian inhibitory GDP/GTP exchange protein (GDI) for smgp25A is active on the yeast SEC4 protein. Mol. Cell. Biol. 11: 2909-2912.

Walworth, N. C., P. Brennwald, A. K. Kabcenell and P. Novick.  1992.  Hydrolysis of GTP by Sec4 protein plays an important role in vesicular transport and is stimulated by a GTPase activating protein in yeast.  Mol. Cell. Biol. 12: 2017-2028.

Novick, P.,  M. Garrett, P. Brennwald and A. Kabcenell. 1992.. Purification of Sec4 protein from S. cerevisiae and E. coli. Methods in Enzymology 219: 352-362.

Potenza, M. R. Bowser, H. Müller and P. Novick.  1992.  SEC6 encodes an 85 kD soluble protein required for exocytosis in yeast.  Yeast 8: 549-558. 

Bowser, R., H. Müller, B. Govindan and P. Novick. 1992.  Sec8p and Sec15p are components of a 19.5S particle that may function downstream of Sec4p to control exocytosis. J. Cell. Biol. 118: 1041-1056.

Jena, B. P., P. Brennwald, M. Garrett, P. Novick and J. D. Jamieson. 1992.  Distinct GAP's in mammalian pancreas act on the yeast GTP-binding proteins Ypt1 and Sec4. FEBS Lett. 309: 5-9.

Moya, M., D. Roberts and P. Novick. 1993.  DSS4-1, is a dominant suppressor of sec4-8 that encodes a nucleotide exchange protein that aids Sec4p function. Nature 361: 460-463.

Burton, J., D. Roberts, M. Montaldi, P. Novick and P. De Camilli. 1993. A mammalian  guanine-nucleotide-releasing protein enhances function of yeast secretory protein Sec4. Nature 361: 464-467.

Brennwald, P. and P. Novick. 1993. Interactions of three domains distinguishing the Ras-related GTP-binding proteins Ypt1 and Sec4. Nature 362: 560-563.

Novick, P., P. Brennwald, N. C. Walworth, A. K. Kabcenell, M. Garrett, M. Moya, D. Roberts, H. Müller, B. Govindan and R. Bowser. 1993. The cycle of SEC4 function in vesicular transport. In "The GTPase superfamily" Wiley, Chichester, Ciba Foundation Symposium 176: 218-232.

Novick, P., P. Brennwald, M. Garrett, M. Moya, D. Roberts, and R. Bowser. 1993. The nucleotide cycle of Sec4 is important for its function in vesicular transport. In "Protein synthesis and targeting in yeast". Pringer-Verlag, NATO ASI Series 71: 325-328.

Novick, P. and P. Brennwald. 1993. Small GTPases and Vesicle Trafficking: Sec4p and its interaction with up and downstream elements. In "GTPases in Biology" B. Dickey and L. Birnbaumer, Editors.

Ferro-Novick, S. and P. Novick.  1993. The role of GTP-binding proteins in transport along the exocytotic pathway. Annual Review of Cell Biology.9: 575-599.

Protopopov, V., B. Govindan, P. Novick, and J. Gerst. 1993. Homologs of the synaptobrevin/VAMP family of synaptic vesicle proteins function on the late secretory pathway in S. cerevisiae. Cell. 74: 855-861.

Garrett, M.D., A.K. Kabcenell, J. Zahner, T. Sasaki, Y. Takai, C. Cheney and P. Novick. 1993. GDP dissociation inhibitor isolated from bovine brain, Drosophila melanogaster or Saccharomyces cerevisiae is active on both Sec4 and Ypt1. FEBS Lett.331: 233-238.

Novick, P. and P. Brennwald. 1993. Friends and family: The role of the Rab GTPases in vesicular traffic. Cell 75: 597-602.

Garrett, M.D., J. Zahner, C. Cheney and P. Novick. 1994. GDI1 encodes a GDP dissociation inhibitor that plays an essential role in the yeast secretory pathway.  EMBO J. 13: 1718-1728.

Novick, P. and Garrett M. D. 1994. Rab attachment - No exchange without receipt. Nature 369: 18-19.

Rothblatt, J., P. Novick and T. Stevens. 1994.  Guidebook to the secretory pathway. Oxford University Press.

Brennwald, P., Kearns, B., Champion, K., Keranen, S., Bankaitis, V. and P. Novick. 1994. Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 79: 245-258.

Govindan, B., R. Bowser and P. Novick. 1995. The role of Myo2p, a yeast type V myosin, in vesicular transport. J. Cell Biol. 128: 1055-1068.

Terbush, D. and P. Novick.  1995. Sec6, Sec8 and Sec15 are components of a multisubunit complex localized to small bud tips in Saccharomyces cerevisiae. J. Cell Biol. 130: 299-312..

Roberts, D. M., M. D. Garrett and P. Novick. 1995. Purification of the GDP dissociation stimulator Dss4 from recombinant bacteria. Methods in Enzymology 257: 84-92.

M. D. Garrett and P. Novick. 1995. Expression, purification and assays of Gdi1p from recombinant E. coli.  Methods in Enzymology 257: 232-240.

Govindan, B. and P. Novick. 1995. Development of cell polarity in budding yeast. J. Exp. Zoo. 273: 401-424

Novick P., M. D. Garrett, P. Brennwald, A. Lauring, F. P. Finger, R. Collins and D. R. TerBush 1995. Control of Exocytosis in Yeast. Cold Spring Harb. Symp. Quant. Biol. 60: 171-177.

De Camilli, P., S.D. Emr, P.S. McPherson and P. Novick 1996. Phosphoinositides as regulators in membrane traffic. Science 271: 1533-1539.

TerBush, D.R., T. Maurice, D. Roth and P. Novick  1996. The Exocyst is a multiprotein complex required for exocytosis in Saccharomyces cerevisiae. EMBO J.15: 6483-6494.

Guo, W., D. Roth, E. Gatti, P. De Camilli and P. Novick 1997. Identification and characterization of homologues of the exocyst component Sec10p. FEBS Letters. 404: 135-139.

Finger, F.P. and P. Novick . 1997. Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae. Mol. Biol. Cell. 8: 647-662.

Walch-Solimena, C., R. Collins and P. Novick.. 1997. Sec2p mediates nucleotide exchange on Sec4p and is involved in polarized delivery of post-Golgi vesicles. J. Cell Biol. 137: 1495-1510.

Collins, N.R., P. Brennwald, M. Garrett, A. Lauring and P. Novick . 1997. Interactions of nucleotide release factor Dss4 with Sec4 in the post-Golgi secretory pathway of yeast. J. Biol. Chem. 272: 18281-18289.

 Novick P. and M. Zerial. 1997. The diversity of Rab proteins in vesicle traffic. Current Opinion in Cell Biology. 9: 496-504.

Du, L.L., R.N. Collins and P. Novick. 1998. Identification of a Sec4p GTPase Activating Protein (GAP) as a novel member of a Rab GAP family. J. Biol. Chem.273: 3253-3256.
Finger, F.P., T.E. Hughes and P. Novick. 1998. Sec3p is a spatial landmark for polarized secretion in budding yeast. Cell 92: 559-571.

Roth, D., W. Guo and P. Novick. 1998. Dominant negative alleles of SEC10 reveal distinct domains involved in secretion and morphogenesis in yeast. Mol. Biol. Cell 9: 1725-1739.

Finger, F.P. and P. Novick. 1998. Spatial regulation of exocytosis: Lessons from yeast. J. Cell Biol. 142: 1-4.

Abeliovich H., E.Grote, P.Novick, S.Ferro-Novick. 1998. Tlg2p, a yeast syntaxin homolog that resides on the Golgi and endocytic structures. J. Biol. Chem.  273:11719-27.

Guo, W., D. Roth, C. Walch-Solimena and P. Novick. 1999. The exocyst is an effector for Sec4p, targeting secretory vesicles to sites of exocytosis. EMBO J. 18: 1071-1080.

Reck-Peterson, S.L., P. Novick, and M.S. Mooseker. 1999. The tail of a yeast class V myosin, Myo2p, functions as a localization domain. Mol. Biol. Cell 10: 1001-1017.

Guo, W., A. Grant and P. Novick. 1999. Exo84p is an exocyst protein essential for secretion. J. Biol. Chem. 274: 23558-23564.

Carr, C.M., E. Grote and P. Novick. 1999. Sec1p binds to SNARE complexes and accumulates at sites of secretion. J. Cell Biol. 146: 333-344.

TerBush, D.R. and P. Novick.  1999. Funnel tube gel protein concentration. J. Biomol. Tech. 10: 149-152.

Walch-Solimena, C. and P. Novick. 1999. The yeast phosphatidylinositol-4-OH kinase Pik1 regulates secretion at the Golgi. Nature Cell Biol. 1: 523-525.

Grote, E and P. Novick. 1999. Promiscuity in Rab/SNARE interactions. Mol. Biol. Cell 10: 4149-4161.

Carr, C.M. and P. Novick. 2000. Changing Partners. Nature. 404:347-349.

Elkind, N.B., C. Walch-Solimena, and P.Novick. 2000. The role of the COOH terminus of Sec2p in the transport of post-Golgi vesicles. J. Cell. Biol. 149: 95-110

Guo, W., M. Sacher, J. Barrowman, S. Ferro-Novick and P. Novick. 2000. Protein complexes in transport vesicle targeting. Trends in Cell Biol. 10: 251-255.

Karpova, T.S., S.L. Reck-Peterson, N.B. Elkind, M.S. Mooseker, P.J. Novick and J.A. Cooper. 2000. Role of actin and Myo2p in polarized secretion and growth of Saccharomyces cerevisiae. Mol. Biol. Cell 11: 1727-1737.

Finger, F.P. and P. Novick. 2000. Synthetic interactions of the post-Golgi sec mutants of Saccharomyces cerevisiae. Genetics 156: 943-951.

Grote, E. and P. Novick. 2000 snc endocytosis mutant: phenotypic analysis and suppression by overproduction of dyhydrosphingosine phosphate lyase. Mol. Biol. Cell 11: 4051-4065.

Lipshutz, J.H., W. Guo, L.E. O’Brien, Y.H. Nguyen, P. Novick, and K.E. Mostov. 2000. The exocyst is involved in cystogenesis and tubulogenesis and acts by modulating synthesis and delivery of basolateral plasma membrane and secretory proteins. Mol. Biol. Cell. 11: 4259-4275.

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

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

Du, L.L. and P. Novick. 2001. Purification and properties of a GTPase-activating protein for yeast Rab GTPases. Meth. Enzymol. 329: 91-99.

TerBush, D.R., W. Guo, S. Dunkelbarger and P. Novick 2001. Purification and characterization of yeast exocyst complex. Meth. Enzymol. 329:100-110.

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

Du, L and P. Novick. 2001. Yeast rab GTPase-activating protein Gyp1p localizes to the Golgi apparatus and is a negative regulator of Ypt1p. Mol. Biol. Cell 12: 1215-1226.

Reck-Peterson, S.L., M.J. Tyska, P. Novick and M.S. Mooseker. 2001 The yeast class V myosins, Myo2p and Myo4p, are non-processive actin based motors. J. Cell Biol. 153: 1121-1126.

Du Y, Pypaert M, Novick P, Ferro-Novick S. 2001Aux1p/Swa2p Is Required for Cortical Endoplasmic Reticulum Inheritance in Saccharomyces cerevisiae. Mol Biol Cell. 12:2614-28.

Drees BL, Sundin B, Brazeau E, Caviston JP, Chen GC, Guo W, Kozminski KG, Lau MW, Moskow JJ, Tong A, Schenkman LR, McKenzie A 3rd, Brennwald P, Longtine M, Bi E, Chan C, Novick P, Boone C, Pringle JR, Davis TN, Fields S, Drubin DG. 2001 A protein interaction map for cell polarity development. J Cell Biol. 154:549-71.

Zhang, X., Bi, E., Novick, P., Du, L., Kozminski, K.G., Lipschutz, J.H. and Guo, W., 2001. Cdc42 interacts with the exocyst and regulates polarized secretion. J. Biol. Chem. 276: 46745-50.

Du, L. and Novick, P. 2002. Pag1p, a novel protein associated with the protein kinase Cbk1p, is required for cell morphogenesis and proliferation in Saccharomyces cerevisiae. Mol. Biol. Cell. 13: 503-514.

Novick, P. and Guo, W. 2002. Ras family therapy: Rab, Rho and Ral talk to the exocyst. Trends in Cell Biol.12: 247-249.

Ortiz, D, Medkova, M., Walch-Solimena, C and 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., and Novick, P. 2003. Sec3p is needed for the spatial regulation of secretion and for the inheritance of the cortical endoplasmic reticulum. Mol. Biol. Cell 14:4770-82

Barrowman,  J. and Novick, P. 2003. Three Yips for Rab Recruitment.  Nat. Cell Biol. 5:955-956.

Kim, J., Estrada, P., Coleman, J., Walker, L., Dunn, B., Takizawa,  P., Novick, P., and Ferro-Novick, S. 2003 Myo4p and She3p are Required for Cortical ER Inheritance in Saccharomyces cerevisiae.  J. Cell Biol. 163:1255-66.

Schekman, R. W. and Novick, P. 2004. Twenty three genes after twenty three years. Cell S116: S13-S15.

Guo, W. and Novick, P. 2004. The exocyst meets the translocon: a regulatory circuit for secretion and protein synthesis? Trends in Cell Biol. 14: 61-63.

Du, Y., Ferro-Novick, S. and Novick, P. 2004. Dynamics and Inheritance of the endoplasmic reticulum.  J. Cell Sci. 117: 2871-2878.

Wiederkehr, A., De Craene, J., Ferro-Novick, S. and Novick, P. 2004. Functional Specialization Within a Vesicle Tethering Complex; Bypass of a Subset of Exocyst Deletion Mutants by Sec1p or Sec4p. J. Cell Biol. 167:875-887.

Boyd, C., Hughes, T., Pypaert, M., and Novick, P. 2004. Vesicles carry most exocyst subunits to exocytic sites marked by the remaining two subunits, Sec3p and Exo70p. J. Cell Biol. 167:889-901.

de Martin, P.E., Du, Y., Novick , P., Ferro-Novick, S. 2005. Ice2p is important for the distribution and structure of the cortical ER network in Saccharomyces cerevisiae.  J. Cell Sci. 118:65-77.

Dong, G., Hutagalung, A.H., Fu. C., Novick, P., Reinisch, K.M. 2005. The structures of Exo70p and the Exo84p C-terminal domains: a common motif and implications for exocyst architecture.  Nature Struc. Mol. Biol. 12:1094-100.

Ortiz, D. and Novick, P. 2006. Ypt32p regulates the translocation of Chs3p from an internal pool to the plasma membrane. Eur. J. Cell Biol. 85:107-16.

France, Y.E., Boyd, C., Coleman, J. and Novick, P. 2006. The polarity scaffold Bem1p regulates the localization of the Exocyst via an interaction with Sec15p. J. Cell Sci.119: 876-88.

Grosshans, B., Andreeva, A., Gangar, A., Niessen, S., Yates, J.R.III, Brennwald, P. and Novick, P. 2006. The yeast lgl family member Sro7p is an effector of the secretory Rab GTPase Sec4p. J. Cell Biol. 172:55-66.

Medkova, M., France,  E., Coleman, J. and Novick, P. 2006. The localization of Sec2p is regulated by its reversible association with the Exocyst. Mol. Biol. Cell 6: 2757-2769.

De Craene, J., Coleman, J., Estrada de Martin, P., Pypaert, M., Anderson, S., Yates, III, J., Ferro-Novick, S., Novick, P. 2006. Rtn1p is involved in structuring the cortical ER. Mol. Biol. Cell 7: 3009-30020.

Munson, M. and Novick, P. 2006. The Exocyst defrocked, a framework of rods revealed. Nat. Struc. Mol. Biol. 13: 577-581.

Grosshans, B., Ortiz, D. and Novick, P. 2006. Rabs and their effectors: Achieving specificity in membrane traffic. Proc. Natl. Acad. Sci. 103: 11821-11827.

Novick, P., Medkova, M., Dong, G., Hutagalung, A., Reinisch, K., and Grosshans, B. 2006. Interactions between Rabs, tethers, SNAREs and their regulators in exocytosis. Biochem. Soc. Trans. 34: 683-686.

Du, Y., Walker, L., Novick, P and Ferro-Novick, S. 2007. Ptc1p regulates cortical ER inheritance via Slt2p. EMBO J. 19: 4413-4422.

Dong, G., Medkova, M., Novick, P. and Reinisch, K. M. 2007. A catalytic coiled coil: structural insights into the activation of the Rab GTPase Sec4p by Sec2p. Mol Cell. 25:455-62.