期刊
DEVELOPMENT
卷 132, 期 15, 页码 3357-3369出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/dev.01916
关键词
oogenesis; meiotic maturation; gamete interactions; major sperm protein signaling; vesicle budding; unconventional protein secretion
资金
- NCI NIH HHS [5P30 CA68485, T32 CA09592] Funding Source: Medline
- NIEHS NIH HHS [5P30 ES00267] Funding Source: Medline
- NIGMS NIH HHS [GM65115, GM57173, R01 GM057173, R01 GM065115] Funding Source: Medline
The major sperm protein (MSP) is the central cytoskeletal element required for actin-independent motility of nematode spermatozoa. MSP has a dual role in Caenorhabditis elegans reproduction, functioning as a hormone for both oocyte meiotic maturation and ovarian muscle contraction. The identification of the signaling function of MSP raised the question, how do spermatozoa, which are devoid of ribosomes, ER and Golgi, release a cytoplasmic protein lacking a signal sequence? Here, we provide evidence that MSP export occurs by the budding of novel vesicles that have both inner and outer membranes with MSP sandwiched in between. MSP vesicles are apparently labile structures that generate long-range MSP gradients for signaling at the oocyte cell surface. Both spermatozoa and non-motile spermatids bud MSP vesicles, but their stability and signaling properties differ. Budding protrusions from the cell body contain MSP, but not the MSD proteins, which counteract MSP filament assembly. We propose that MSP generates the protrusive force for its own vesicular export.
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