We found a match
Your institution may have access to this item. Find your institution then sign in to continue.
- Title
Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre.
- Authors
Xiaoling Tang; Jianchao Zhang; Ying Cai; Shiying Miao; Shudong Zong; Koide, S. S.; Linfang Wang
- Abstract
hSMP-1 is a human sperm membrane protein expressed during development. It is a testis-specific component produced during male germ cell differentiation. Proteins that interact with hSMP-1 were identified by the application of the yeast two-hybrid system. One of the components, RanBPM, was found to be associated with hSMP-1 under both in vitro and in vivo conditions. In the human testis, RanBPM is produced in spermatogonia and primary spermatocytes, suggesting expression during the early stages of spermatogenesis; whereas in the rat testis, it is located in round and elongated spermatids, similar to hSMP-1, suggesting expression of both components during spermiogenesis. Images obtained by immunofluorescence and confocal scanning microscopy of CHO-K1 cells co-transfected with pEGFP-C1-hSMP-1 and pDsRed1-Nl-RanBPM revealed that RanBPM and hSMP-1 are distributed in discrete loci throughout the cytoplasm. When superimposed, the stained spots appeared as congruent yellow areas, indicative of co-localization and probable complex formation of these two components. This interaction between hSMP-1 and RanBPM may be involved in the process of male germ cell differentiation. In CHO-Kl cells transfected with pEGFP-Cl-hSMP-1, the exogenously expressed hSMP-1 was found to co-localize with α-tubulin. Depolymerization of microtubules can be induced in CHO-Kl cells by cold treatment. In cells transfected with the pEGFP-Cl vector, the dispersed tubulins promptly reassembled upon warming. However, in cells transfected with pEGFP-Cl-hSMP-1, reassembly of the dispersed tubulins was blocked even upon rewarming of the cells. These findings suggest that hSMP-1 interacts with tubulins and thereby may modulate microtubule assembly and/or activity.
- Subjects
MEMBRANE proteins; SPERMATOZOA; GERM cells; SPERMATOGENESIS in animals; MALE reproductive organs; CELL differentiation
- Publication
Journal of Molecular Medicine, 2004, Vol 82, Issue 6, p383
- ISSN
0946-2716
- Publication type
Article
- DOI
10.1007/s00109-004-0535-2