A protein interaction map for cell polarity development

Drees, Becky; Sundin, Bryan A.; Brazeau, Elizabeth; Caviston, Juliane P.; Chen, Guang Chao; Guo, Wei; Kozminski, Keith G.; Lau, M.; Moskow, John J.; Tong, Amy; Schenkman, Laura R.; Mckenzie, Amos; Brennwald, Patrick; Longtine, Mark S.; Bi, Erfei; Chan, Chung Chow; Novick, Peter; Boone, Charles; Pringle, John R.; Davis, Trisha N.; Fields, Stanley; Drubin, David G.

doi:10.1083/jcb.200104057

Cited by 290 publications

(269 citation statements)

References 182 publications

(281 reference statements)

Supporting

Mentioning

246

Contrasting

Unclassified

Order By: Relevance

“…Immunoprecipitation experiments on HeLa cells stimulated or not with purified InlB using antibodies for SEPT9 or Met did not reveal a direct interaction between Met and SEPT9 (our unpublished observations). However, very few direct interaction partners have been identified for septins [Drees et al, 2001], possibly because septin-binding partners interact with specific conformations of higher order septin assemblies and not with individual septins or septin complexes [Barral and Kinoshita, 2008].…”

Section: Septins Modulate Bacterial Entry Into Host Cellsmentioning

confidence: 99%

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

Mostowy

Cossart

2009

Cell Motil. Cytoskeleton

View full text Add to dashboard Cite

The study of an infection process can reveal how microbes exploit the host, and can illuminate unknown host cellular functions. Invasive pathogens have evolved efficient strategies to promote their internalization within normally non-phagocytic host cells. The so-called ''zippering'' bacteria present to host cell receptors molecules that mimic endogenous ligands, thereby inducing specific intracellular signaling cascades ultimately resulting in actin polymerization and uptake. Here we review how the bacterial pathogen Listeria monocytogenes enters into cells, and present a series of studies revealing that in addition to actin rearrangements this bacterium exploits the clathrin-mediated endocytosis machinery together with septins, a novel cytoskeleton element. The challenge is now to decipher how all of these components orchestrate themselves to permit entry into normally non-phagocytic cells. Cell Motil. Cytoskeleton 66: 816-823, 2009. '

show abstract

Section: Septins Modulate Bacterial Entry Into Host Cellsmentioning

confidence: 99%

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

Mostowy

Cossart

2009

Cell Motil. Cytoskeleton

View full text Add to dashboard Cite

show abstract

“…The templates for integration were pDH3 and pHAB102 (Drees et al, 2001;Abeliovich et al, 2002). Normal prApe1 processing and vacuolar morphology were used to confirm the functionality of all genomic fusions.…”

Section: Strains and Mediamentioning

confidence: 99%

Early Stages of the Secretory Pathway, but Not Endosomes, Are Required for Cvt Vesicle and Autophagosome Assembly inSaccharomyces cerevisiae

Reggiori

Wang

Nair

et al. 2004

MBoC

129

163

View full text Add to dashboard Cite

The Cvt pathway is a biosynthetic transport route for a distinct subset of resident yeast vacuolar hydrolases, whereas macroautophagy is a nonspecific degradative mechanism that allows cell survival during starvation. Yet, these two vacuolar trafficking pathways share a number of identical molecular components and are morphologically very similar. For example, one of the hallmarks of both pathways is the formation of double-membrane cytosolic vesicles that sequester cargo before vacuolar delivery. The origin of the vesicle membrane has been controversial and various lines of evidence have implicated essentially all compartments of the endomembrane system. Despite the analogies between the Cvt pathway and autophagy, earlier work has suggested that the origin of the engulfing vesicle membranes is different; the endoplasmic reticulum is proposed to be required only for autophagy. In contrast, in this study we demonstrate that the endoplasmic reticulum and/or Golgi complex, but not endosomal compartments, play an important role for both yeast transport routes. Along these lines, we demonstrate that Berkeley bodies, a structure generated from the Golgi complex in sec7 cells, are immunolabeled with Atg8, a structural component of autophagosomes. Finally, we also show that none of the yeast t-SNAREs are located at the preautophagosomal structure, the presumed site of double-membrane vesicle formation. Based on our results, we propose two models for Cvt vesicle biogenesis. INTRODUCTIONThe lysosome/vacuole is the major cellular center for degradation, recycling, and storage of biological constituents. Several well-characterized transport routes are implicated in protein delivery to this organelle during normal growth conditions. These pathways are conserved among eukaryotic organisms, but work in the yeast Saccharomyces cerevisiae has had a major impact on their characterization and in the identification of the molecular machinery (Conibear and Stevens, 1998). The route called the alkaline phosphatase pathway provides a direct transport connection between the Golgi complex and the vacuole Piper et al., 1997). A second itinerary from the Golgi complex to the vacuole passes through the late endosome and is known as the carboxypeptidase Y pathway (Piper et al., 1995;Babst et al., 1998;Conibear and Stevens, 1998). These two pathways are required for the biogenesis and maintenance of vacuoles, whereas a third route, endocytosis, has a catabolic function. Endocytosis mediates the downregulation of plasma membrane proteins by delivering them via the late endosome to the vacuole for degradation (Hicke, 1999;Katzmann et al., 2002). Before reaching the late endosome, these proteins pass through the early endosome where some components are recycled back to the cell surface (Hicke et al., 1997;Prescianotto-Baschong and Riezman, 1998;Lewis et al., 2000). The carboxypeptidase Y pathway and endocytosis converge at the endosome where another route, the multivesicular body pathway, delivers both resident enzymes and substrates to the vac...

show abstract

“…It is becoming clear that the ADF/cofilin (AC) family of proteins, which catalyze actin-filament severing and depolymerization in cells (reviewed by Moon and Drubin, 1995;Sarmiere and Bamburg, 2003;Zigmond, 2004), is necessary for cell migration (reviewed by Bamburg and Wiggan, 2002). AC proteins are also known regulators of cell polarity, both in yeast (Drees et al, 2001;Okada et al, 2006) and also in migrating cell types, both to sustain already established polarity (Dawe et al, 2003) and to trigger cell polarization (Helen R. Dawe. The role of ADF/cofilin family proteins in the acquisition and maintenance of cell polarity during fibroblast migration.…”

Section: Introductionmentioning

confidence: 99%

ADF/cofilin family proteins control formation of oriented actin-filament bundles in the cell body to trigger fibroblast polarization

Mseka

Bamburg

Cramer

2007

Journal of Cell Science

View full text Add to dashboard Cite

How formation of the front and rear of a cell are coordinated during cell polarization in migrating cells is not well understood. Time-lapse microscopy of live primary chick embryo heart fibroblasts expressing GFP-actin show that, prior to cell polarization, polymerized actin in the cell body reorganizes to form oriented actin-filament bundles spanning the entire cell body. Within an average of 5 minutes of oriented actin bundles forming, localized cell-edge retraction initiates at either the side or at one end of the newly formed bundles and then elaborates around the nearest end of the bundles to form the cell rear, the first visual break in cell symmetry. Localized net protrusion occurs at the opposing end of the bundles to form the cell front and lags formation of the rear of the cell. Consequently, cells acquire full polarity and start to migrate in the direction of the long axis of the bundles, as previously documented for already migrating cells. When ADF/cofilin family protein activity or actin-filament disassembly is specifically blocked during cell polarization, reorganization of polymerized actin to form oriented actin-filament bundles in the cell body fails, and formation of the cell rear and front is inhibited. We conclude that formation of oriented actin-filament bundles in the cell body requires ADF/cofilin family proteins, and is an early event needed to coordinate the spatial location of the cell rear and front during fibroblast polarization.

show abstract

A protein interaction map for cell polarity development

Cited by 290 publications

References 182 publications

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

Cytoskeleton rearrangements during Listeria infection: Clathrin and septins as new players in the game

Early Stages of the Secretory Pathway, but Not Endosomes, Are Required for Cvt Vesicle and Autophagosome Assembly inSaccharomyces cerevisiae

ADF/cofilin family proteins control formation of oriented actin-filament bundles in the cell body to trigger fibroblast polarization

Contact Info

Product

Resources

About