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Mary Porter, Ph.D.

Professor

Mailing Address:
University of Minnesota
Department of Genetics, Cell Biology, and Development
6-160 Jackson
321 Church St. SE
Minneapolis, MN 55455
USA
Education:
Ph.D., 1982, University of Pennsylvania, Philadelphia, PA
Office:
4-106 MCB
P: 612-626-1901

Email:
porte001@umn.edu

 Lab:
4-224 MCB
P: 612-626-2621

Areas of Research Strength:

Cytoskeleton
Cell motility

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Research Techniques:

Cell fractionation and protein biochemistry
Molecular genetics (insertional mutagenesis and gene recovery)
Classical genetics (genetic screens and phenotypic analysis)
High resolution electron microscopy and computer image averaging
DIC and epifluorescence light microscopy, video imaging

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Research Interests:

Research in the Porter lab is focused on the function and regulation of
the dynein motors. Dyneins are microtubule-associated ATPases that
are responsible for minus-end directed movement of cellular cargoes on
the microtubule cytoskeleton. Defects in the dyneins or associated regulatory
proteins have significant consequences for an organism. In vertebrates, these
include infertility, chronic respiratory disease, polycystic kidney disease, and
defects in the development of the left-right body axis. We use a combination
of molecular, genetic, and structural techniques in a simple model organism,
Chlamydomonas reinhardtii, to identify members of the dynein gene family,
to determine where they are located inside cells, to identify their specific cargoes,
and to understand how the cell regulates the activity of its multiple dynein motors.
Because dynein associated proteins are highly conserved between species, we can
then identify homologous genes in higher organisms and analyze their full range
of functions. Current projects in the laboratory are focused on two major topics.

1) Regulation of the flagellar motility. The lab has used both classical genetics
and insertional mutagenesis to isolate several novel genes involved in the regulation
of dynein arm activity and flagellar motility. Characterization of the gene products
suggests that many of the polypeptides serve as structural scaffolds for the attachment
of regulatory enzymes that modify the phosphorylation state of the dyneins. We are
using a combination of protein biochemistry and molecular genetics to further characterize
these interactions. These studies will provide new insights into how the activity of multiple
dynein motors can be coordinated and regulated within a single cell.

2) Characterization of motor proteins involved in flagellar assembly. The lab has identified
a novel dynein isoform, cDhc1b, as an unusual cytoplasmic dynein that is required for
flagellar assembly in Chlamydomonas. The function of the cDhc1b motor as the retrograde
motor for intraflagellar transport appears to be conserved in all ciliated organisms. We have
recently identified a new subunit of the cDhc1b complex, as well as several mutations that
modify the activity of the cDhc1b motor. We are characterizing the distribution of the gene
products in Chlamydomonas by biochemical methods and immunocytochemistry. The
distribution of these gene products is also being analyzed in mammalian cells and tissues
to better understand the their function in more complex organisms.


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Selected Publications:

Nicastro, D., Schwartz, C., Pierson, J., Gaudette, R., Porter, M.E., and J. R. McIntosh (2006) The molecular architecture of axonemes revealed by cryoelectron tomography.  Science 313:944-948.

Pfister, KK, Fisher, EM, Gibbons, IR, Hays, TS, Holzbaur, EL, McIntosh, JR, Porter, ME, Schroer, TA, Vaughan, KT, Witman, GB, King, SM, and Vallee RB. (2006) Cytoplasmic dynein nomenclature, J. Cell Biol. 171:411-413.

Mueller J, Perrone CA, Bower R, Cole DG, and ME Porter (2005) The FLA3 KAP subunit is required for localization of Kinesin-2 to the site of flagellar assembly and processive anterograde intrafagellar transport. Mol. Biol. Cell 16:1341-1354.

Hendrickson TW, Perrone CA, Griffin P, Wuichet K, Mueller J, Yang P, Porter ME, WS Sale (2004) IC138 is a WD-repeat dynein intermediate chain required for light chain assembly and regulation of flagellar bending. Mol. Biol. Cell 15:5431-5442.

Rupp, G., and M.E. Porter (2003) A subunit of the dynein regulatory complex in Chlamydomonas is a homologue of a growth arrest specific gene product. J. Cell Biol. 162:47-57.

Perrone CA, Tritschler D, Taulman P, Bower R, Yoder BK, Porter ME. (2003) A novel Dynein light intermediate chain colocalizes with the retrograde motor for intraflagellar transport at sites of axoneme assembly in Chlamydomonas and mammalian cells. Mol Biol Cell. 14:2041-56.

Rupp, G., E.T. O'Toole, and M.E. Porter (2001) The Chlamydomonas PF6 locus encodes a large, alanine/proline rich polypeptide required for assembly of a central pair projection and regulates flagellar motility. Mol. Biol. Cell 12:739-751

Perrone, C.A., S.H. Myster, R. Bower, E.T. O'Toole, and M.E. Porter (2000) Insights into the structural organization of the I1 inner arm dynein from a domain analysis of the 1b dynein heavy chain. Mol. Biol. Cell 11: 2297-2313

Porter, M.E. and W.S. Sale (2000) The 9 + 2 axoneme anchors multiple inner arm dyneins and a network of kinases and phophatases that control motility. J. Cell Biol. 151:F37-F42

Porter, M.E., R. Bower, J.A. Knott, P. Byrd, and W. Dentler (1999) Cytoplasmic dynein heavy chain 1b is required for flagellar assembly in Chlamydomonas. Mol. Biol. Cell 10:693-712.

Myster, S.H., J.A. Knott, K.M. Wysocki, E. OíToole, and M.E. Porter (1999) Domains in the 1 alpha dynein heavy chain required for inner arm assembly and flagellar motility in Chlamydomonas. J. Cell Biol. 146:801-818.

Norrander, J.M., A.M. deCathelineau, J.A. Brown, M.E. Porter, and R.W. Linck (1999) The rib43a protein is associated with forming the specialized protofilament ribbons of flagellar microtubules in Chlamydomonas. Mol. Biol. Cell. 11:201-215.

C. A. Perrone, P. Yang, E. OíToole, and M.E. Porter (1998) The Chlamydomonas IDA7 locus encodes a 140-kDa dynein intermediate chain required to assemble the I1 inner arm complex. Mol. Biol. Cell 9:3351-3365.

S. Myster, J. Knott, E. OíToole, and M. E. Porter (1997) The Chlamydomonas Dhc1 gene encodes a dynein heavy chain subunit required for the assembly of the I1 inner arm complex. Mol. Biol. Cell 8:607-620.

Porter, M.E. (1996) Axonemal dyneins: assembly, organization, and regulation. Curr. Opin. Cell Biol. 8:10-17.

Porter, M. E., J. Knott, S. Myster, and S. Farlow, (1996) Characterization of the dynein gene family in Chlamydomonas. Genetics144:569-585.

Rupp, G., E. O'Toole, L.C. Gardner, B. Mitchell, and M.E. Porter (1996) The sup-pf-2 mutations of Chlamydomonas alter the activity of the outer dynein arm by modification of the gamma heavy chain. J. Cell Biol. 135:1853-1865.

Gardner, L.C., E. O'Toole, C. Perrone, T. Giddings, and M.E. Porter (1994) Components of a "dynein regulatory complex" are located at the junction between the radial spokes and dyneins arms in Chlamydomonas flagella. J. Cell Biol. 127:1311-1324.

Reviews:
Wirschell, M., Nicastro, D., Porter, M.E., and W.S. Sale (2007) Structural basis for regulation of flagellar motility: organization of the dynein regulatory complex, inter-dynein linkers and a network of axonemal kinases and phosphatases.  In Chlamydomonas Source Book, 2nd Edition, Vol. III (G. B. Witman, editor). In press.



To view these and other publications visit http://www.ncbi.nlm.nih.gov/PubMed
search menu should say PubMed
type Porter ME in the avaliable line

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 Last modified on Thursday, July 26, 2007