Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase

Science

Volumn 299, Issue 5610, 2003, Pages 1231-1235

  Wedlich Soldner, Roland ^a   Altschuter, Steve ^b   Wu, Lani ^b   Li, Rong ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

^b HARVARD UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

FEEDBACK; PLASMA APPLICATIONS; POLARIZATION; POLYMERIZATION; PROBABILITY; YEAST;

CELL POLARIZATION;

CELLS;

ACTIN; CELL CYCLE PROTEIN; GUANOSINE TRIPHOSPHATASE; MYOSIN ADENOSINE TRIPHOSPHATASE; PROTEIN CDC42; UNCLASSIFIED DRUG;

BIOCHEMISTRY; POLYMERIZATION;

ACTIN FILAMENT; ACTIN POLYMERIZATION; ARTICLE; CELL MEMBRANE; CELL POLARITY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME RELEASE; MATHEMATICS; NONHUMAN; POSITIVE FEEDBACK; PRIORITY JOURNAL; PROBABILITY; SIMULATION; STOCHASTIC MODEL; YEAST;

ACTINS; ACTOMYOSIN; CDC42 GTP-BINDING PROTEIN, SACCHAROMYCES CEREVISIAE; CELL MEMBRANE; CELL POLARITY; COMPUTER SIMULATION; CUES; G1 PHASE; GUANOSINE TRIPHOSPHATE; INTRACELLULAR MEMBRANES; MICROFILAMENTS; MICROSCOPY, CONFOCAL; MODELS, BIOLOGICAL; MUTATION; PROTEIN TRANSPORT; SACCHAROMYCES CEREVISIAE; SECRETORY VESICLES;

EID: 0037458909     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1080944     Document Type: Article

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32. We thank P. Crews for latrunculin A; A. Amon, A. Bretscher, S. Emr, C. Kaiser, and P. Novick for reagents and yeast strains; J. Waters-Shuler and the Nikon Imaging Center for help on confocal microscopy; and M. D. Altschuler, J. Gunawardena, M. Kirschner, T. Michison, A. Murray, E. Conlon, B. Ward, and S. Wedlich for advice and comments on the manuscript. Supported by an EMBO fellowship (R.W.S.) and by NIH grant GM057063 (R.L.).