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Trina A. Schroer
Professor
Department of Biology
Graduate Program Faculty
B.S.
Stanford University
Ph.D.
University of California, San Francisco
Postdoctoral
Washington University, School of Medicine |
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Department of Biology
Johns Hopkins University
3400 North Charles Street
Baltimore, MD 21218-2685
U.S.A. |
Office Telephone:
Lab Telephone:
Lab Fax:
Email: |
410.516.5373
410.516.5374,0179
410.516.5375
schroer@jhu.edu |

Office- Mudd 220A
Lab - Mudd 203 |
[Research Interests] [Honors] [Representative Publications] [Lab
Members]
RESEARCH INTERESTS
Microtubule-Based Motors and Cytoarchitecture
My lab is interested in how microtubule-based motors contribute to a subcellular organization and motility. Our work focuses on
the motor, cytoplasmic dynein, and its activator, dynactin. Together, these proteins provide the majority of minus end-directed
motor activity in interphase cells. Dynein and dynactin drive the centripetal movement of the endomembrane systems that support
membrane protein biosynthesis and recycling, and also contribute significantly to the organization of the microtubule cytoskeleton
during interphase and mitosis. Both dynein and dynactin are large, multisubunit complexes. Dynein provides the "brawn" for
movement, while dynactin acts as the "brains" that controls motility, serving as both a linker between dynein and its
cargoes, and as a processivity factor that allows dynein to move over longer distances. Because dynein's cargoes include structures
as diverse as membranes, microtubules, chromosomes and possibly cell signaling molecules, we are interested in understanding the
mechanisms by which dynactin interacts with each.
To better understand dynein and dynactin structure and function, our lab has taken broad approach, using biochemical,biophysical,
molecular biological and microscopy-based techniques. To study dynactin function in vivo, we work in the model systems of
fibroblasts, neurons, polarized epithelia and phagocytic cells, each of which highlights a different type of dynein-based motility.
Using sophisticated microscopy techniques, we study subcellular dynamics in vivo and in vitro.
Biochemical and molecular biological methods have provided us with large quantities of native dynactin and recombinant subunits
for enzymological, structural and biophysical studies. These efforts have provided a clear picture of dynactin subunit organization.
The dynein and cargo binding subdomains of dynactin have been identified and we are in the process of defining cargo receptors and
the molecular details of the dynein-dynactin and dynactin-microtubule interaction.

HONORS
2006 Alumni Association Excellence in Teaching Award from the Krieger School for a course on AIDS (020.347).
Representative Publications
Berezuk, M.A., and Schroer, T.A. 2007. Dynactin is a processivity factor for kinesin-2. Traffic. 8:124-129.
Schramm B, de Haan CA, Young J, Doglio L, Schleich S, Reese C, Popov AV, Steffen W, Schroer T, Locker JK. 2006. Vaccinia-Virus-Induced Cellular Contractility Facilitates the Subcellular Localization of the Viral Replication Sites. Traffic.
Imai H, Narita A, Schroer TA, Maeda Y. 2006. Two-dimensional averaged images of the dynactin complex revealed by single particle analysis. J Mol Biol. Jun 16;359(4):833-9.
Brown CL, Maier KC, Stauber T, Ginkel LM, Wordeman L, Vernos I, Schroer TA. 2005. Kinesin-2 is a motor for late endosomes and lysosomes. Traffic. (12):1114-24.
Pfister KK, Fisher EM, Gibbons IR, Hays TS, Holzbaur EL, McIntosh JR, Porter ME, Schroer TA, Vaughan KT, Witman GB, King SM, Vallee RB. 2005. Cytoplasmic dynein nomenclature. J Cell Biol. 71(3):411-3.
Schroer TA. 2004. Dynactin. Annu Rev Cell Dev Biol. 20:759-79. Review.
Berezuk, M., and Schroer, T.A. 2004. Isolation and characterization of
native kinesin II from brain. Traffic, 5, 503-513.
King SJ, Brown CL, Maier KC, Quintyne NJ, Schroer TA. 2003. Analysis of the dynein-dynactin interaction in vitro and in vivo. Mol Biol Cell.14(12):5089-97.
Eckley, D.M. and Schroer, T.A. 2003. Interactions between the
evolutionarily conserved, actin-related protein, Arp11, actin and Arp1. Mol. Biol. Cell, 14, 2645-2654.
Goodson HV, Skube SB, Stalder R, Valetti C, Kreis TE, Morrison EE, Schroer TA. 2003. CLIP-170 interacts with dynactin complex and the APC-binding protein EB1 by different mechanisms. Cell Motil Cytoskeleton. 55(3):156-73.
Quintyne, N.J. and Schroer, T.A. 2002. Distinct cell cycle-dependent
roles for dynactin and dynein at centrosomes. J. Cell Biol., 159,
245-254.
Salina, D., Boldoor, K., Eckley, D.M., Schroer, T.A., Rattner, J.B.,
Burke, B. 2002. Cytoplasmic dynein as a facilitator of nuclear envelope
breakdown. Cell, 108, 97-107.
Habermann, A., Schroer, T.A., Griffiths, G. and Burkhardt, J. K. 2001. Immunolocalization of cytoplasmic dynein and
dynactin subunits in cultured macrophages: Enrichment on early endocytic organelles, J. Cell Sci., 114, 229-240.
Schroer, T.A,. 2001. Microtubules don and doff their caps: dynamic attachments at microtubule ends. Curr. Op.
Cell Biol., 13, 92-93.
King, S.J. and Schroer, T.A. 2000. Dynactin increases the processivity of the cytoplasmic dynein motor. Nature Cell Biology, 2, 20-24.
Lab Members
Graduate Students:
Frances Cheong Seamus Levine-Wilkinson
Brett Scipioni
Postdoctoral Fellow:
Ting-Yu Yeh
Undergraduate Researcher:
Daniel Oh
Lab Helper
David Yoo
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