Karin Reinisch, PhD
David W. Wallace Professor of Cell Biology and of Molecular Biophysics and Biochemistry; Director of Graduate Studies
Research & Publications
Biography
News
Research Summary
molecular mechanisms underlying membrane trafficking and lipid homeostasis.
Coauthors
Selected Publications
- Lipid scrambling is a general feature of protein insertasesLi D, Rocha-Roa C, Schilling M, Reinisch K, Vanni S. Lipid scrambling is a general feature of protein insertases. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2319476121. PMID: 38621120, PMCID: PMC11047089, DOI: 10.1073/pnas.2319476121.
- Spartin-mediated lipid transfer facilitates lipid droplet turnoverWan N, Hong Z, Parson M, Korfhage J, Burke J, Melia T, Reinisch K. Spartin-mediated lipid transfer facilitates lipid droplet turnover. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2314093121. PMID: 38190532, PMCID: PMC10801920, DOI: 10.1073/pnas.2314093121.
- The Role of VPS13 and Related Proteins in lipid transport at membrane contact sitesReinisch K. The Role of VPS13 and Related Proteins in lipid transport at membrane contact sites. The FASEB Journal 2021, 35 DOI: 10.1096/fasebj.2021.35.s1.00089.
- Control of plasma membrane lipid homeostasis by the extended synaptotagminsSaheki Y, Bian X, Schauder CM, Sawaki Y, Surma MA, Klose C, Pincet F, Reinisch KM, De Camilli P. Control of plasma membrane lipid homeostasis by the extended synaptotagmins. Nature Cell Biology 2016, 18: 504-515. PMID: 27065097, PMCID: PMC4848133, DOI: 10.1038/ncb3339.
- The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membraneBaskin JM, Wu X, Christiano R, Oh MS, Schauder CM, Gazzerro E, Messa M, Baldassari S, Assereto S, Biancheri R, Zara F, Minetti C, Raimondi A, Simons M, Walther TC, Reinisch KM, De Camilli P. The leukodystrophy protein FAM126A (hyccin) regulates PtdIns(4)P synthesis at the plasma membrane. Nature Cell Biology 2015, 18: 132-138. PMID: 26571211, PMCID: PMC4689616, DOI: 10.1038/ncb3271.
- The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing MotifsHorenkamp FA, Kauffman KJ, Kohler LJ, Sherwood RK, Krueger KP, Shteyn V, Roy CR, Melia TJ, Reinisch KM. The Legionella Anti-autophagy Effector RavZ Targets the Autophagosome via PI3P- and Curvature-Sensing Motifs. Developmental Cell 2015, 34: 569-576. PMID: 26343456, PMCID: PMC4594837, DOI: 10.1016/j.devcel.2015.08.010.
- Re-visiting the trans insertion model for complexin clampingKrishnakumar SS, Li F, Coleman J, Schauder CM, Kümmel D, Pincet F, Rothman JE, Reinisch KM. Re-visiting the trans insertion model for complexin clamping. ELife 2015, 4: e04463. PMID: 25831964, PMCID: PMC4384536, DOI: 10.7554/elife.04463.
- Sac1–Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatusCai Y, Deng Y, Horenkamp F, Reinisch KM, Burd CG. Sac1–Vps74 structure reveals a mechanism to terminate phosphoinositide signaling in the Golgi apparatus. Journal Of Cell Biology 2014, 206: 485-491. PMID: 25113029, PMCID: PMC4137058, DOI: 10.1083/jcb.201404041.
- Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transferSchauder CM, Wu X, Saheki Y, Narayanaswamy P, Torta F, Wenk MR, De Camilli P, Reinisch KM. Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer. Nature 2014, 510: 552-555. PMID: 24847877, PMCID: PMC4135724, DOI: 10.1038/nature13269.
- Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivationLangemeyer L, Bastos R, Cai Y, Itzen A, Reinisch KM, Barr FA. Diversity and plasticity in Rab GTPase nucleotide release mechanism has consequences for Rab activation and inactivation. ELife 2014, 3: e01623. PMID: 24520163, PMCID: PMC3919270, DOI: 10.7554/elife.01623.
- The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathwayTan D, Cai Y, Wang J, Zhang J, Menon S, Chou HT, Ferro-Novick S, Reinisch KM, Walz T. The EM structure of the TRAPPIII complex leads to the identification of a requirement for COPII vesicles on the macroautophagy pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: 19432-19437. PMID: 24218626, PMCID: PMC3845172, DOI: 10.1073/pnas.1316356110.
- Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrateWu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 18672-18677. PMID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.
- A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusionKrishnakumar SS, Radoff DT, Kümmel D, Giraudo CG, Li F, Khandan L, Baguley SW, Coleman J, Reinisch KM, Pincet F, Rothman JE. A conformational switch in complexin is required for synaptotagmin to trigger synaptic fusion. Nature Structural & Molecular Biology 2011, 18: 934-940. PMID: 21785412, PMCID: PMC3668341, DOI: 10.1038/nsmb.2103.
- Structure and function of the polymerase core of TRAMP, a RNA surveillance complexHamill S, Wolin SL, Reinisch KM. Structure and function of the polymerase core of TRAMP, a RNA surveillance complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 15045-15050. PMID: 20696927, PMCID: PMC2930566, DOI: 10.1073/pnas.1003505107.
- Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexesVasan N, Hutagalung A, Novick P, Reinisch KM. Structure of a C-terminal fragment of its Vps53 subunit suggests similarity of Golgi-associated retrograde protein (GARP) complex to a family of tethering complexes. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 14176-14181. PMID: 20660722, PMCID: PMC2922553, DOI: 10.1073/pnas.1009419107.
- Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase HeterodimerDong G, Wearsch PA, Peaper DR, Cresswell P, Reinisch KM. Insights into MHC Class I Peptide Loading from the Structure of the Tapasin-ERp57 Thiol Oxidoreductase Heterodimer. Immunity 2009, 30: 21-32. PMID: 19119025, PMCID: PMC2650231, DOI: 10.1016/j.immuni.2008.10.018.
- The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering ComplexesCai Y, Chin HF, Lazarova D, Menon S, Fu C, Cai H, Sclafani A, Rodgers DW, De La Cruz EM, Ferro-Novick S, Reinisch KM. The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes. Cell 2008, 133: 1202-1213. PMID: 18585354, PMCID: PMC2465810, DOI: 10.1016/j.cell.2008.04.049.
- A Catalytic Coiled Coil: Structural Insights into the Activation of the Rab GTPase Sec4p by Sec2pDong G, Medkova M, Novick P, Reinisch KM. A Catalytic Coiled Coil: Structural Insights into the Activation of the Rab GTPase Sec4p by Sec2p. Molecular Cell 2007, 25: 455-462. PMID: 17289591, PMCID: PMC1847580, DOI: 10.1016/j.molcel.2007.01.013.
- Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigenFuchs G, Stein AJ, Fu C, Reinisch KM, Wolin SL. Structural and biochemical basis for misfolded RNA recognition by the Ro autoantigen. Nature Structural & Molecular Biology 2006, 13: 1002-1009. PMID: 17041599, DOI: 10.1038/nsmb1156.
- The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motifDong G, Hutagalung AH, Fu C, Novick P, Reinisch KM. The structures of exocyst subunit Exo70p and the Exo84p C-terminal domains reveal a common motif. Nature Structural & Molecular Biology 2005, 12: 1094-1100. PMID: 16249794, DOI: 10.1038/nsmb1017.
- Structural Insights into RNA Quality Control: The Ro Autoantigen Binds Misfolded RNAs via Its Central CavityStein AJ, Fuchs G, Fu C, Wolin SL, Reinisch KM. Structural Insights into RNA Quality Control: The Ro Autoantigen Binds Misfolded RNAs via Its Central Cavity. Cell 2005, 121: 529-539. PMID: 15907467, PMCID: PMC1769319, DOI: 10.1016/j.cell.2005.03.009.
- Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patchDong G, Chakshusmathi G, Wolin SL, Reinisch KM. Structure of the La motif: a winged helix domain mediates RNA binding via a conserved aromatic patch. The EMBO Journal 2004, 23: 1000-1007. PMID: 14976553, PMCID: PMC380972, DOI: 10.1038/sj.emboj.7600115.