14-3-3 and its binding partners are regulators of protein-protein interactions during spermatogenesis

被引:35
|
作者
Sun, Shengyi [1 ]
Wong, Elissa W. P. [1 ]
Li, Michelle W. M. [1 ]
Lee, Will M. [2 ]
Cheng, C. Yan [1 ]
机构
[1] Populat Council, Ctr Biomed Res, Mary M Wohlford Lab Male Contracept Res, New York, NY 10065 USA
[2] Univ Hong Kong, Sch Biol Sci, Hong Kong, Hong Kong, Peoples R China
基金
美国国家卫生研究院;
关键词
APICAL ECTOPLASMIC SPECIALIZATION; PHOSPHORYLATED NITRATE REDUCTASE; COMPREHENSIVE PROTEOMIC ANALYSIS; GERM CELL-INTERACTIONS; JUNCTION DYNAMICS; SEMINIFEROUS EPITHELIUM; IN-VIVO; CONTRACEPTIVE DEVELOPMENT; ENDOPLASMIC-RETICULUM; MEMBRANE-PROTEINS;
D O I
10.1677/JOE-09-0041
中图分类号
R5 [内科学];
学科分类号
1002 ; 100201 ;
摘要
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 in adult rat testes. This event coincides with the migration of preleptotene/leptotene spermatocytes across the blood-testis barrier from the basal to the apical (or adluminal) 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 begin meiosis I to be followed by meiosis 11 to form spermatids (haploid, In) at stage XIV of the epithelial cycle. 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 have 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. Journal of Endocrinology (2009) 202, 327-336
引用
收藏
页码:327 / 336
页数:10
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