Accession Number:

ADA434009

Title:

Regulation of Cdc42/Rac Signaling in the Establishment of Cell Polarity and Control of Cell Motility

Descriptive Note:

Annual summary rept. 1 Aug 2001-31 Jul 2004

Corporate Author:

DUKE UNIV MEDICAL CENTER DURHAM NC

Personal Author(s):

• Irazoqui, Javier E.

Report Date:

2004-08-01

Pagination or Media Count:

66.0

Abstract:

Cdc42p, together with other polarity proteins, becomes polarize to a cap at the presumptive bud site and the tip of the emerging bud. The initial observation that Cdc42p is able to polarize, and remain polarized, in the complete absence of F-actin Ayscough et al., 1997, has been confirmed repeatedly by many laboratories including ours. These studies use Lat-A as a quick, effective method to completely depolymerize actin, and led to the conclusion that Cdc42p polarization is actin-independent. Polarized secretion and endocytic uptake require F-actin cables and patches, respectively. When Lat-A is applied to yeast cells, neither actin patches nor cables are detectable, and all F-actin-dependent processes are disrupted. Thus, Cdc42p polarization occurs by a non-secretory pathway.

Descriptors:

• *BREAST CANCER
• POLARIZATION
• MEMBRANES(BIOLOGY)
• POLYMERIZATION
• PROTEINS
• CELLS(BIOLOGY)
• POLARITY
• MUSCLE PROTEINS

Subject Categories:

• Biochemistry
• Anatomy and Physiology
• Medicine and Medical Research

Distribution Statement:

APPROVED FOR PUBLIC RELEASE