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This Article Accepted manuscript (PDF) All Versions of this Article: JOE-09-0041v1 202/3/327    most recent Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Sun, I. Articles by Cheng, C Y Search for Related Content PubMed PubMed Citation Articles by Sun, I. Articles by Cheng, C Y

I Sun, Population Council, New York, United States
E Wong, Population Council, New York, United States
M Li, Population Council, New York, United States
W Lee, School of Biological Sciences, Hong Kong, Hong Kong
C Cheng, Center for Biomedical Research, Population Council, New York, 10021, United States

Correspondence: C Y Cheng, Email: y-cheng{at}popcbr.rockefeller.edu

During spermatogenesis, spermiation takes place at the adluminal edge of the seminiferous epithelium at stage VIII of the epithelial cycle during which fully developed spermatids (i.e., spermatozoa) detach from the epithelium. This event coincides with the migration of preleptotene/leptotene spermatocytes across the blood-testis barrier (BTB) from the basal to the apical compartment. At stage XIV of the epithelial cycle, pachytene spermatocytes (diploid, 2n) differentiate into diplotene spermatocytes (tetraploid, 4n) in the apical compartment of the epithelium, which will begin meiosis I to be followed by meiosis II to form spermatids (haploid, 1n). These spermatids, in turn, undergo extensive morphological changes and traverse the seminiferous epithelium until they differentiate into elongated spermatids. Thus, there are extensive changes at the Sertoli-Sertoli and Sertoli-germ cell interface via protein ‘coupling’ and ‘uncoupling’ between cell adhesion protein complexes, as well as changes in interactions between integral membrane proteins and their peripheral adaptors, regulatory protein kinases and phosphatases, and the cytoskeletal proteins. These precisely coordinated protein-protein interactions affect cell adhesion and cell movement. In this review, we focus on the 14-3-3 protein family, whose members are having different binding partners in the seminiferous epithelium. Recent studies have illustrated that 14-3-3 affects protein-protein interactions in the seminiferous epithelium, and regulates cell adhesion possibly via its effects on intracellular protein trafficking and cell polarity proteins. This review provides a summary on the latest findings regarding the role of 14-3-3 family of proteins and their potential implications on spermatogenesis. We also highlight research areas that deserve attentions by investigators.

This article has been cited by other articles:

				E. W. P. Wong, S. Sun, M. W. M. Li, W. M. Lee, and C. Y. Cheng 14-3-3 Protein Regulates Cell Adhesion in the Seminiferous Epithelium of Rat Testes Endocrinology, October 1, 2009; 150(10): 4713 - 4723. [Abstract] [Full Text] [PDF]