Interactions among IQGAP1, Cdc42, and the cadherin/catenin protein complex regulate Sertoli-germ cell adherens junction dynamics in the testis

Journal of Cellular Physiology
Wing Yee LuiC Yan Cheng

Abstract

The movement of developing germ cells across the seminiferous epithelium during spermatogenesis involves extensive adherens junction (AJ) restructuring between Sertoli cells, as well as between Sertoli and germ cells. In this report, we show that the intricate interactions between Cdc42 (a Rho family protein of Mr approximately 23 kDa originally identified in membranes of human platelets and placenta, and is the homolog of CDC42Sc, which is known to regulate of bud-site assembly in Saccharomyces cerevisiae) and its effector, IQ motif containing GTPase activating protein (IQGAP1, Mr approximately 189 kDa, it is also an actin-binding protein known to interact with Cdc42 and Rac1 GTPases), regulate Sertoli-germ cell, but not Sertoli-Sertoli cell, AJ dynamics. Using testis lysates for immunoprecipitation (IP), IQGAP1 was shown to associate with E-cadherin, N-cadherin, and beta-catenin (but not beta1-integrin and nectin-2), as well as with actin and vimentin (but not alpha-tubulin). Moreover, IQGAP1 was found to localize to the periphery of both Sertoli and germ cells in the seminiferous epithelium, at sites of cell-cell contacts. Using fluorescent microscopy with dual fluorescent probes, IQGAP1 was found to co-localize, at least in...Continue Reading

References

Apr 9, 1990·FEBS Letters·Y L ChanI G Wool
Jan 1, 1985·International Review of Cytology·L D Russell, R N Peterson
Jul 1, 1996·Journal of Cellular Physiology·G R AravindanC Y Cheng
Nov 15, 1996·Genomics·P W Marks, D J Kwiatkowski
Jun 30, 1997·The Journal of Cell Biology·A M BashourG S Bloom
Sep 26, 1997·The Journal of Biological Chemistry·J W EricksonM J Hart
Dec 31, 1997·The Journal of Biological Chemistry·M FukataK Kaibuchi
Dec 29, 1998·The Journal of Biological Chemistry·Y D HoD B Sacks
Aug 17, 1999·Biochemical and Biophysical Research Communications·S KurodaK Kaibuchi
Sep 3, 1999·The Journal of Biological Chemistry·M FukataK Kaibuchi
Sep 10, 1999·The Journal of Biological Chemistry·D D Mruk, C Y Cheng
Dec 23, 1999·The Journal of Biological Chemistry·Z LiD B Sacks
Apr 19, 2000·Archives of Histology and Cytology·A W VoglJ Guttman
Jan 12, 2001·Physiological Reviews·Y TakaiT Matozaki
Mar 15, 2001·Current Opinion in Cell Biology·J W Erickson, R A Cerione
Dec 6, 2001·The Journal of Biological Chemistry·Michael W BriggsDavid B Sacks
Feb 13, 2003·Biochimica Et Biophysica Acta·Wing-Yee LuiC Yan Cheng
Mar 18, 2003·Endocrinology·Ann S N Lau, Dolores D Mruk
Apr 12, 2003·Anatomical Science International·Yoshiro ToyamaShigeki Yuasa
Dec 24, 2004·Endocrine Reviews·Knut KrohnRalf Paschke

❮ Previous
Next ❯

Citations

Jul 26, 2005·Histochemistry and Cell Biology·Nobuo TeradaShinichi Ohno
Sep 24, 2008·In Vitro Cellular & Developmental Biology. Animal·Brianna C PranteJ Suzanne Lindsey
Apr 21, 2010·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Ilona A KoperaDolores D Mruk
Jan 13, 2010·Cold Spring Harbor Perspectives in Biology·Werner W Franke
May 17, 2008·Pharmacological Reviews·Dolores D MrukC Yan Cheng
Apr 3, 2009·Sexual Development : Genetics, Molecular Biology, Evolution, Endocrinology, Embryology, and Pathology of Sex Determination and Differentiation·A P SinghY Mishina
Oct 25, 2007·International Journal of Cancer. Journal International Du Cancer·Shun-Hua JinYasuhito Yuasa
Dec 7, 2010·International Journal of Andrology·Y-H LinP-L Kuo
Mar 18, 2015·Chemical Biology & Drug Design·Muhammad Imran QadirMuhammad Ali
Jul 19, 2005·Cytokine & Growth Factor Reviews·Weiliang XiaC Yan Cheng
Dec 11, 2007·Biochimica Et Biophysica Acta·Elissa W P WongC Yan Cheng
Jan 24, 2013·Critical Reviews in Biochemistry and Molecular Biology·Wenhui SuC Yan Cheng
Sep 17, 2014·Seminars in Cell & Developmental Biology·Miguel Quiros, Asma Nusrat
Jun 14, 2016·Seminars in Cell & Developmental Biology·Ying GaoC Yan Cheng
Oct 10, 2009·International Review of Cell and Molecular Biology·Elissa W P Wong, C Yan Cheng
Oct 14, 2006·Molecular Reproduction and Development·Markus LassilaHarry Holthöfer
Dec 29, 2005·The Journal of Biological Chemistry·Polly J Phillips-MasonSusann M Brady-Kalnay
Feb 28, 2015·EMBO Reports·Andrew C HedmanDavid B Sacks
Jan 10, 2017·International Journal of Molecular Sciences·Ying-Hung LinChung-Hsin Yeh
Sep 20, 2006·Cancer Research·Laurent BalenciJacques Baudier
Jan 13, 2021·Biomedicine & Pharmacotherapy = Biomédecine & Pharmacothérapie·Xiafeng PengYan Zhang
Mar 18, 2020·Biochemical and Biophysical Research Communications·Ivan LimanjayaTzu-Jen Kao
Aug 19, 2021·Cell Reports·Yoshifumi MoriTakashi Shinohara

❮ Previous
Next ❯

Related Concepts

Related Feeds

Adhesion Molecules in Health and Disease

Cell adhesion molecules are a subset of cell adhesion proteins located on the cell surface involved in binding with other cells or with the extracellular matrix in the process called cell adhesion. In essence, cell adhesion molecules help cells stick to each other and to their surroundings. Cell adhesion is a crucial component in maintaining tissue structure and function. Discover the latest research on adhesion molecule and their role in health and disease here.

Adherens Junctions

An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques). Adherens junctions uniquely disassemble in uterine epithelial cells to allow the blastocyst to penetrate between epithelial cells. Discover the latest research on adherens junctions here.

Actin-binding Proteins

Actin-binding proteins are a component of the actin cytoskeleton that play essential roles in cellular functions such as regulation of actin polymerization, maintenance of cell polarity, gene expression regulation, cell motility and many more functions. Discover the latest research on actin-binding proteins here.

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.