Researchers

Angela Fleischhacker

Research Investigator

afleisch@umich.edu

734-615-6150

Carmen Gherasim, Ph.D.

Research Investigator

gherasim@umich.edu

734-764-4461

Omer Kabil, Ph.D.

Assistant Research Scientist

omerk@umich.edu

734-764-4461

Jyoti Malhotra, Ph.D.

Adjunct Research Investigator, Internal Medicine

shubi@umich.edu

734-936-4785

Manolo Plasencia

Research Fellow

plasenci@umich.edu

734-763-3130

Henriette Remmer, Ph.D.

Director, Proteomics & Peptide Synthesis Core

Assistant Research Scientist, Biological Chemistry

hremmer@umich.edu

734-763-6285

Jeanne Stuckey, Ph.D.

Associate Professor, Life Sciences Institute

Research Associate Professor, Biological Chemistry

Associate Professor, Biophysics

jass@umich.edu

734-647-7532

Victor Vitvitsky, Ph.D.

Research Assistant Professor

victorv@umich.edu

(734) 764-4461

Spotlight

Vps13 and Cdc31/centrin: Puzzling partners in membrane traffic

Vps13 (Vacuolar Protein Sorting 13) proteins, conserved in all eukaryotes, are high molecular weight polypeptides (>3000 aa) that function in vesicular trafficking and fusion, spore membrane expansion and fusion, autophagy and phagocytosis and at organelle membrane contact sites. Each of four widely-expressed human homologs, VPS13A-D, is the locus of a distinct autosomal recessive neurodegenerative or neurodevelopment disease. A collaborative study from the Fuller and Skiniotis labs, recently published in the Journal of Cell Biology (http://jcb.rupress.org/content/early/2017/01/31/jcb.201606078) and noted in a spotlight mini-review (http://jcb.rupress.org/content/early/2017/01/24/jcb.201612026), reveals that functional yeast Vps13 protein exists as a complex with the small Ca2+ binding protein Cdc31/centrin and folds into an unusual, unitary handle-loop structure. The protein contains conserved domains that possess binding sites for phosphatidic acid, PI3P and PI4,5P2. These lipid binding characteristics may explain the ability of Vps13 to interact with a wide array of organelle membranes and to act as an effector of set of seemingly unrelated intermembrane transactions.

Read the JCB Article Here: