Jawdat Al-Bassam
ASSISTANT PROFESSOR
jawdat@ucdavis.edu
Molecular & Cellular Biology
Office
Life Science Addition-3220
530-752-3521
Lab
Life Sciences Addition-3215
Degrees:
2011
Post Doctoral Fellow
Harvard Medical School
2004
PhD
Scripps Research Institute
Biochemistry and Biophysics
1998
BS
California State University Long Beach
Biochemistry
Research Interests:
The Structure and Mechanisms of Microtubule Regulatory Proteins in Assembly and Disassembly of tubulin dimers
Microtubules are dynamic polymers that are critical for many physical transformations that cells undergo in order to divide, develop, or generate motility. Microtubules assemble from basic building blocks, called alpha beta (αβ) tubulin dimers, which polymerize head-to-tail to form protofilaments, using the energy of Guanosine 3,5 Triphosphate (GTP) binding and hydrolysis; These tubulin protofilaments associate laterally enclosing a tube-like structure-- a microtubule. Tubulin polymerization activates GTP hydrolysis only within the microtubule wall and leads to stochastic events called catastrophes, in which protofilaments peel ane curl to disassemble the microtubule structure. The dynamics of tubulin heterodimer assembly and disassembly into microtubules occurs at the ends of microtubules, and are highly regulated by conserved types of proteins that are found in all organisms. These proteins, in effect, act as MT “Polymerases” and “Depolymerases” accelerating the slow processes of polymerization and depolymerization that tubulin dimers can carry-out alone. The laboratory is focused on deciphering the mechanisms of these microtubule regulatory proteins and how they cooperate to regulate microtubule dynamics in highly synchronized cellular phenomena like cell division and development. The physical scale of microtubule dynamics can be studied multiple approaches that span a great resolution scale span from micro-meters to the sub-nanometer scale. The Laboratory combines biochemistry, structural biology approaches such as electron microscopy and X-ray crystallography, with high resolution single molecule total internal reflection microscopy to study the mechanisms of Microtubule Polymerases and Depolymerases at multiple levels of spatial and temporal resolution.
Awards:
National Institutes of Health Pathway to Independence award 2008-2014
American Cancer Society Postdoctoral Fellowship 2005-2008
American Heart Association Predoctoral Fellowship 1999-2002
California State University President's Scholarship 1995-1998
Professional Societies:
American Society of Cell Biology
American Biophysical Society
CBS Graduate Group Affiliations:
Biochemistry, Molecular, Cellular and Developmental Biology
Biophysics
Specialties / Focus:
Biochemistry, Molecular, Cellular and Developmental Biology
Publications:
Last updated 1/19/2012
Al-Bassam J , Chang F. Regulation of Microtubule dynamics by TOG domain proteins XMAP215/Dis1 and CLASP. Trends in Cell Biology, 2011. 21 (10): 604-614
Al-Bassam J , Kim H, Brouhard G, van Oijen A, Harrison SC, Chang F. CLASP promotes microubule rescues by recruiting tubulin dimer to the microtubule” . Developmenal Cell, 2010. 19 (2): 245--258
Brouhard G*, Stear J* , Notzel T, Al-Bassam J, Kinoshita K, Harrison SC, Howard J, Hyman AA, XMAP215 is a processive microtubule polymerase that catalyzes both growth and shrinkage, Cell. 2008, 132(1):79-88;
Al-Bassam J, Larsen NA, Hyman AA, Harrison SC. Crystal structure of a TOG domain: conserved features of XMAP215/Dis1-family TOG domains and implications for tubulin binding. Structure. 2007 Mar; 15(3):355-62.
Al-Bassam J, Roger B, Halpain S, Milligan RA. Analysis of the weak interactions of ADP-Unc104 and ADP-kinesin with microtubules and their inhibition by MAP2c. Cell Motil Cytoskeleton. 2007 May;64(5):377-89
Larsen NA, Al-Bassam J, Wei RR, Harrison SC. Structural analysis of Bub3 interactions in the mitotic spindle checkpoint. Proc Natl Acad Sci U S A. 2007 Jan 23;104(4):1201-6.
Wei RR, Al-Bassam J, Harrison SC. The Ndc80/HEC1 complex is a contact point for kinetochoremicrotubule attachment. Nat Struct Mol Biol. 2007 Jan;14(1):54-9.
Al-Bassam J*, van Breugel M*, Harrison SC, Hyman A. Stu2p binds tubulin and undergoes an open-to closed conformational change. J Cell Biol. 2006 Mar 27; 172:1009-22.
Roger. B*, Al-Bassam J.*, Milligan R.A., Halpain S. MAP2, but not tau, repeats bind and bundle factin, Current Biol. 2004. 14:363-371
Al-Bassam J.*, Cui Y.*, Klopheinstein D., Carragher, B.O., Vale R.D., Milligan, R.A. Distinct Conformations of the Kinesin Unc104 Neck Regulate a Monomer-to-Dimer Motor Transition, J. CellBiol. 2003. 163: 743-753.
Al-Bassam J., Ozer R.S., Safer D., Halpain S., Milligan R.A.; MAP2 and tau bind along the outer ridges of microtubule protofilaments. 2002. J. Cell Biol. 157: 1187-1196.
Key Words:
Microtubule, Tubulin, biochemistry, Cryo-electron microscopy, x-ray crystallography