Jawdat Al-Bassam

image of Jawdat Al-Bassam

ASSISTANT PROFESSOR

Departments

Molecular & Cellular Biology

Offices and Labs

Life Science Addition-3220
530-752-3521
Life Sciences Addition-3215

Degrees

2011 Post Doctoral Fellow Harvard Medical School
2004 PhD Biochemistry and Biophysics Scripps Research Institute
1998 BS Biochemistry California State University Long Beach

Research Contribution

1) Molecular mechanisms of multi-subunit assemblies modulating the biogenesis, polymerization into microtubule polymers. 2) Molecular mechanisms of mitotic motor proteins in alignment and organization of mitotic spindles during cell division.

Research Interests

The Structure and Mechanisms of Microtubule Regulatory Proteins in Assembly and Disassembly of tubulin dimers

Microtubules are dynamic protein polymers that generate forces inside eukaryotic cells that lead to transformations to divide, develop, or crawl. Microtubules assemble from basic building blocks, known as 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 protofilaments associate laterally enclosing a tube-like structure-- a microtubule. Tubulin polymerization is driven by its high concentration inside the cytoplasm and activates GTP hydrolysis upon its incorporation into microtubule lattices at their ends.  However, during stochastic reversals, called catastrophes, tubulin protofilaments stop polymerizing and peel-out to rapidly dissemble microtubules. The Al-Bassam laboratory studies conserved multi-subunit molecular machines drive soluble ab-tubulin heterodimers biogenesis inside cells, and how ab-tubulins are polymerized or depolymerized at microtubule ends.  These molecular machines are found in all eukaryotic organisms and act as ab-tubulin “factories”, microtubule “polymerases” or “depolymerases” to accelerate specific aspects of microtubule dynamics inside cells. We are focused on deciphering mechanisms of these machines and how they cooperate during cell division and development. We combine biochemistry, structural biology approaches such as electron microscopy and X-ray crystallography with high-resolution single molecule total internal reflection microscopy to study the structure and regulation of microtubule dynamics.  These powerful approaches bridge the large resolution range between ab-tubulin structure  and its polymerization into dynamic microtubules, which span micro-meters to the sub-nanometers.   These approaches allow us to link  atomic architectures of these molecular machines with ab-tubulin and their conformational changes during unique functional states at microtubule ends.

Awards

Hellman Fellow University of California Davis, 2014
University of California Cancer Research Coordinating Committee Award, 2013-2014
National Institutes of Health Pathway to independence award 2008-2014
American Cancer Society Postdoctoral Fellowship 2005-2008
American Heart Association Predoctoral Fellowship 2000-2003
National Institutes of Health Pathway to independence Award 2008-2014
California State University President's Scholarship 1995-1998

Department and Center Affiliations

UC-Davis Comphrensive Cancer Center

ProfessionalSocieties

American Society of Cell Biology
American Biophysical Society

CBS Grad Group Affiliations

Biochemistry, Molecular, Cellular and Developmental Biology
Biophysics

Specialties / Focus

Biochemistry, Molecular, Cellular and Developmental Biology
  • Biochemistry
  • Cell Biology
  • Cell Division and the Cytoskeleton
  • Structural Biology

Labs

al-bassam lab website

Courses

MCB 143 Cell Biophysics (Spring)

Publications

8/21/2014 11:15:59 AM
  • Nithiananatham S, Le S, Seto E, Jia W, Leary J, Corbett KD, Moore JK, Al-Bassam J Tubulin Cofactors and Arl2 are Cage-like Chaperones that regulate the soluble αβ-Tubulin pool for Microtubule Dynamics. eLife (Cambridge) 2015;10.7554/eLife.08811

  • Scholey J.E., Nithiananatham S., Scholey J.M., Al-Bassam J. “The structural basis for the Assembly of the Mitotic Motor Kinesin-5 into Bipolar Tetramers”. Elife (Cambridge). 2014.  3:e02217. doi: 10.7554/elife.02217

  • Al-Bassam J. ”Reconstituting Dynamic Microtubule Polymerization Regulation by TOG Domain Proteins”. Methods in Enzymology. 2014. 540: 131-14
  • Al-Bassam J. ”Reconstituting Dynamic Microtubule Polymerization Regulation by TOG Domain Proteins”. Methods in Enzymology. 2014. 540: 131-14
  • Al-Bassam J., Corbett K. α-Tubulin Acetylation from the inside out . PNAS. 2012. 109:19515-19516.
  • Al-Bassam J., Kim H., Flor-Parra I., Lal N., Velji H., Chang F. Fission yeast Alp14 is a Dose Dependent Plus end-tracking Microtubule Polymerase. Mol Biol Cell. 23:2878-2890.
  • 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.