ArticleJournal of molecular medicine (Berlin, Germany)2004
Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre.
Article in Journal of molecular medicine (Berlin, Germany), 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 16 citations in OpenAlex.
- Ran-binding protein M is associated with human spermatogenesis and oogenesis.Molecular medicine reports · 2018Article
- Cell signalling pathway regulation by RanBPM: molecular insights and disease implications.Open biology · 2017Review
- RanBPM, a scaffolding protein for gametogenesis.Current topics in developmental biology · 2013Review
- Role of microRNAs in controlling gene expression in different segments of the human epididymis.PloS one · 2012Article
- Intracellular proadrenomedullin-derived peptides decorate the microtubules and contribute to cytoskeleton function.Endocrinology · 2008Article
- Netrin-1 mediates neuronal survival through PIKE-L interaction with the dependence receptor UNC5B.Nature cell biology · 2008Article
- RanBPM, a scaffolding protein in the immune and nervous systems.Journal of neuroimmune pharmacology : the official journal of the Society on NeuroImmune Pharmacology · 2007Review
Corrections and comments
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Authors and funding
7 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 alpha-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.
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