Regulation of Cell-Cell Adhesion by Rho Family GTPases

2005 ◽  
pp. 157-189
Author(s):  
Astrid Kraemer ◽  
Alpha S. Yap
Keyword(s):  
Cell Adhesion ◽  
Rho Family Gtpases ◽  
Rho Family ◽  
Cell Cell

Rho-family GTPases in cadherin-mediated cell — cell adhesion

2001 ◽  
Vol 2 (12) ◽  
pp. 887-897 ◽  
Author(s):  
Masaki Fukata ◽  
Kozo Kaibuchi
Keyword(s):  
Cell Adhesion ◽  
Rho Family Gtpases ◽  
Rho Family ◽  
Cell Cell

Regulation of cadherin-mediated cell–cell adhesion by the Rho family GTPases

1999 ◽  
Vol 11 (5) ◽  
pp. 591-596 ◽  
Author(s):  
Kozo Kaibuchi ◽  
Shinya Kuroda ◽  
Masaki Fukata ◽  
Masato Nakagawa
Keyword(s):  
Cell Adhesion ◽  
Rho Family Gtpases ◽  
Rho Family ◽  
Cell Cell

Effects of Rho Family GTPases on Cell-Cell Adhesion

2003 ◽  
pp. 121-128
Author(s):  
Masaki Fukata ◽  
Masato Nakagawa ◽  
Shinya Kuroda ◽  
Kozo Kaibuchi
Keyword(s):  
Cell Adhesion ◽  
Rho Family Gtpases ◽  
Rho Family ◽  
Cell Cell

scholarly journals Regulation of Rho Family GTPases by Cell-Cell and Cell-Matrix Adhesion

2002 ◽  
Vol 35 (2) ◽  
Author(s):  
WILLIAM T. ARTHUR ◽  
NICOLE K. NOREN ◽  
KEITH BURRIDGE
Keyword(s):  
Matrix Adhesion ◽  
Cell Matrix ◽  
Rho Family Gtpases ◽  
Rho Family ◽  
Cell Matrix Adhesion ◽  
Cell Cell

scholarly journals The CEACAM1-L Glycoprotein Associates with the Actin Cytoskeleton and Localizes to Cell–Cell Contact through Activation of Rho-like GTPases

2000 ◽  
Vol 11 (1) ◽  
pp. 65-77 ◽  
Author(s):  
Svetlana Sadekova ◽  
Nathalie Lamarche-Vane ◽  
Xiaodong Li ◽  
Nicole Beauchemin
Keyword(s):  
Cell Adhesion ◽  
Actin Cytoskeleton ◽  
Adhesion Molecule ◽  
Control Cell ◽  
Growth Inhibitor ◽  
Cytoplasmic Domain ◽  
Cell Contact ◽  
A Cell ◽  
Rho Family ◽  
Cell Cell

Associations between plasma membrane-linked proteins and the actin cytoskeleton play a crucial role in defining cell shape and determination, ensuring cell motility and facilitating cell–cell or cell–substratum adhesion. Here, we present evidence that CEACAM1-L, a cell adhesion molecule of the carcinoembryonic antigen family, is associated with the actin cytoskeleton. We have delineated the regions involved in actin cytoskeleton association to the distal end of the CEACAM1-L long cytoplasmic domain. We have demonstrated that CEACAM1-S, an isoform of CEACAM1 with a truncated cytoplasmic domain, does not interact with the actin cytoskeleton. In addition, a major difference in subcellular localization of the two CEACAM1 isoforms was observed. Furthermore, we have established that the localization of CEACAM1-L at cell–cell boundaries is regulated by the Rho family of GTPases. The retention of the protein at the sites of intercellular contacts critically depends on homophilic CEACAM1–CEACAM1 interactions and association with the actin cytoskeleton. Our results provide new evidence on how the Rho family of GTPases can control cell adhesion: by directing an adhesion molecule to its proper cellular destination. In addition, these results provide an insight into the mechanisms of why CEACAM1-L, but not CEACAM1-S, functions as a tumor cell growth inhibitor.

scholarly journals The Small GTPases Rho and Rac Are Required for the Establishment of Cadherin-dependent Cell–Cell Contacts

1997 ◽  
Vol 137 (6) ◽  
pp. 1421-1431 ◽  
Author(s):  
Vania M.M. Braga ◽  
Laura M. Machesky ◽  
Alan Hall ◽  
Neil A. Hotchin
Keyword(s):  
Cell Adhesion ◽  
Epithelial Cells ◽  
Active Form ◽  
Intercellular Junctions ◽  
Small Gtpases ◽  
Cell Contacts ◽  
Calcium Dependent ◽  
Dependent Cell ◽  
Rho Family ◽  
Cell Cell

Cadherins are calcium-dependent cell–cell adhesion molecules that require the interaction of the cytoplasmic tail with the actin cytoskeleton for adhesive activity. Because of the functional relationship between cadherin receptors and actin filament organization, we investigated whether members of the Rho family of small GTPases are necessary for cadherin adhesion. In fibroblasts, the Rho family members Rho and Rac regulate actin polymerization to produce stress fibers and lamellipodia, respectively. In epithelial cells, we demonstrate that Rho and Rac are required for the establishment of cadherin-mediated cell–cell adhesion and the actin reorganization necessary to stabilize the receptors at sites of intercellular junctions. Blocking endogenous Rho or Rac selectively removed cadherin complexes from junctions induced for up to 3 h, while desmosomes were not perturbed. In addition, withdrawal of cadherins from intercellular junctions temporally precedes the removal of CD44 and integrins, other microfilament-associated receptors. Our data showed that the concerted action of Rho and Rac modulate the establishment of cadherin adhesion: a constitutively active form of Rac was not sufficient to stabilize cadherindependent cell–cell contacts when endogenous Rho was inhibited. Upon induction of calcium-dependent intercellular adhesion, there was a rapid accumulation of actin at sites of cell–cell contacts, which was prevented by blocking cadherin function, Rho or Rac activity. However, if cadherin complexes are clustered by specific antibodies attached to beads, actin recruitment to the receptors was perturbed by inhibiting Rac but not Rho. Our results provide new insights into the role of the small GTPases in the cadherin-dependent cell– cell contact formation and the remodelling of actin filaments in epithelial cells.

scholarly journals Activated PAK4 Regulates Cell Adhesion and Anchorage-Independent Growth

2001 ◽  
Vol 21 (10) ◽  
pp. 3523-3533 ◽  
Author(s):  
Jian Qu ◽  
Marta S. Cammarano ◽  
Qing Shi ◽  
Kenneth C. Ha ◽  
Primal de Lanerolle ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Rho Gtpase ◽  
Morphological Changes ◽  
Focal Adhesions ◽  
Dominant Negative ◽  
Oncogenic Transformation ◽  
Wild Type ◽  
Focus Formation ◽  
Rho Family Gtpases ◽  
Rho Family

ABSTRACT The serine/threonine kinase PAK4 is an effector molecule for the Rho GTPase Cdc42. PAK4 differs from other members of the PAK family in both sequence and function. Previously we have shown that an important function of this kinase is to mediate the induction of filopodia in response to activated Cdc42. Since previous characterization of PAK4 was carried out only with the wild-type kinase, we have generated a constitutively active mutant of the kinase to determine whether it has other functions. Expression of activated PAK4 in fibroblasts led to a transient induction of filopodia, which is consistent with its role as an effector for Cdc42. In addition, use of the activated mutant revealed a number of other important functions of this kinase that were not revealed by studying the wild-type kinase. For example, activated PAK4 led to the dissolution of stress fibers and loss of focal adhesions. Consequently, cells expressing activated PAK4 had a defect in cell spreading onto fibronectin-coated surfaces. Most importantly, fibroblasts expressing activated PAK4 had a morphology that was characteristic of oncogenic transformation. These cells were anchorage independent and formed colonies in soft agar, similar to what has been observed previously in cells expressing activated Cdc42. Consistent with this, dominant-negative PAK4 mutants inhibited focus formation by oncogenic Dbl, an exchange factor for Rho family GTPases. These results provide the first demonstration that a PAK family member can transform cells and indicate that PAK4 may play an essential role in oncogenic transformation by the GTPases. We propose that the morphological changes and changes in cell adhesion induced by PAK4 may play a direct role in oncogenic transformation by Rho family GTPases and their exchange factors.

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