Karin M. Reinisch, Ph.D.

Associate Professor of Cell Biology We combine structural biology and biochemistry techniques to better understand the molecular mechanisms underlying cell function, with a main focus on membrane trafficking and the secretory pathway.
Phone: (203) 785-6469 Lab: (203) 785-6027 Fax: (203) 785-7446 e-mail: karin dot reinisch at yale dot edu Lab web site: www.cellbiology.yale.edu/reinisch		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-212a/214 New Haven, CT 06510-3206

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We are interested in the molecular mechanisms that underlie important cellular processes. Currently our major effort is focused on the assembly and regulation of large protein complexes involved in secretory trafficking, the membrane tethering complexes.  There are two additional projects in the laboratory having to do with RNA quality control and MHC class I antigen presentation.

1. Membrane trafficking.

2. RNA/protein interactions, particularly those involved in the processing and quality control of non-coding RNAs.

3. The MHC class I peptide loading complex.

 

Click for a larger image. A space filling representation of the Ro protein in complex with a fragment of Y RNA and single stranded RNA. Ro, a major lupus autoantigen, is normally found bound to a small cytoplasmic RNA, a Y RNA. In the nucleus, Ro also binds to misfolded RNAs and likely targets them for degradation. These misfolded RNAs bind both on the Y RNA binding surface of Ro and, by means of single stranded extensions, in the central cavity of Ro.

Click for a larger image. diffraction image from a crystal of unliganded Ro. The crystal diffracts to beyond 2Å.

 

Recent Publications

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Cai, H., Reinisch, K., Ferro-Novick, S. (2007) Coats, Tethers, Rabs and SNAREs work together to mediate the intracellular destination of a transport vesicle.
Dev Cell. 2007 May; 12(5):671-82

Reinisch, KM., Wolin, SL., Emerging themes in non-coding RNA quality control.
Curr Opin Struct Biol. 2007 Apr; 17(2):209-14. Epub 2007 Mar 28.

Dong, G., Medkova, M., Novick, P., Reinisch, KM. A catalytic coiled coil:structural insights into the activation of the Rab GTPase. Sec4p by Sec2p. Mol Cell. 2007 Feb 9; 25(3):455-62.

Cai, H., Yu, S., Menon, S., Cai, Y., Lazarova, D., Fu, C., Reinisch, K., Hay, JC., Feroo-Novick, S.  TRAPPI Tethers COPII vesicles by binding the coat subunit Sec23. Nature. 2007 Feb 22; 445(7130):941-4. Epub 2007 Feb 7.

Fuchs, G., Stein, A.J., Fu, C. , Reinisch, K.M., and Wolin, S.L. (2006) structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen.
Nat Struct Mol Biol. 2006 Nov;13(11):1002-9. Epub 2006 Oct 15.

Dong G, Hutagalung AH, Fu C, Novick P, Reinisch, KM. (2005)  The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nat Struct Mol Biol. 12(12):1094-100.   

Stein AJ, Fuchs G, Fu C, Wolin SL, Reinisch KM. (2005). Structural insights into RNA quality control: The Ro autoantigen binds misfolded RNAs via its central cavity. Cell 121: 529-539. 

Dong G, Chakshusmathi G, Wolin SL, Reinisch KM. (2004)  Structure of the La motif: a winged helix motif mediates RNA binding via a conserved patch. EMBO J. 23(5):1000-7. 

Reinisch KM. (2002)  The dsRNA viridae and their catalytic capsids. Nat Struct Biol 9: 714-716. (News & Views) 

Reinisch KM, Nibert ML, Harrison SC. (2000)  Structure of the reovirus core at 3.6Å resolution. Nature 404: 960-967.  

Luongo CL, Reinisch KM, Harrison SC, Nibert ML. (2000)  Identification of the guanylyl-transferase region and active site in reovirus mRNA capping protein lambda2. J Mol Biol. 275: 2804-2810.  
Reinisch KM, Chen L, Verdine GL, Lipscomb WN. (1995)  The crystal structure of HaeIII methyltransferase covalently complexed to DNA: an extrahelical cytosine & rearranged base pairing. Cell 82(1): 143-153.