LEM-domain proteins are lost during human spermiogenesis but BAF and BAF-L persist. Issue 4 (October 2017)
- Record Type:
- Journal Article
- Title:
- LEM-domain proteins are lost during human spermiogenesis but BAF and BAF-L persist. Issue 4 (October 2017)
- Main Title:
- LEM-domain proteins are lost during human spermiogenesis but BAF and BAF-L persist
- Authors:
- Elkhatib, Razan A
Paci, Marine
Boissier, Romain
Longepied, Guy
Auguste, Yasmina
Achard, Vincent
Bourgeois, Patrice
Levy, Nicolas
Branger, Nicolas
Mitchell, Michael J
Metzler-Guillemain, Catherine - Abstract:
- Abstract : During spermiogenesis the spermatid nucleus is elongated, and dramatically reduced in size with protamines replacing histones to produce a highly compacted chromatin. After fertilisation, this process is reversed in the oocyte to form the male pronucleus. Emerging evidence, including the coordinated loss of the nuclear lamina (NL) and the histones, supports the involvement of the NL in spermatid nuclear remodelling, but how the NL links to the chromatin is not known. In somatic cells, interactions between the NL and the chromatin have been demonstrated: LEM-domain proteins and LBR interact with the NL and respectively, the chromatin proteins BAF and HP1. We therefore sought to characterise the lamina-chromatin interface during spermiogenesis, by investigating the localisation of six LEM-domain proteins, two BAF proteins and LBR, in human spermatids and spermatozoa. Using RT-PCR, IF and western blotting, we show that six of the proteins tested are present in spermatids: LEMD1, LEMD2 (a short isoform), ANKLE2, LAP2β, BAF and BAF-L, and three absent: Emerin, LBR and LEMD3. The full-length LEMD2 isoform, required for nuclear integrity in somatic cells, is absent. In spermatids, no protein localised to the nuclear periphery, but five were nucleoplasmic, receding towards the posterior nuclear pole as spermatids matured. Our study therefore establishes that the lamina-chromatin interface in human spermatids is radically distinct from that defined in somatic cells. InAbstract : During spermiogenesis the spermatid nucleus is elongated, and dramatically reduced in size with protamines replacing histones to produce a highly compacted chromatin. After fertilisation, this process is reversed in the oocyte to form the male pronucleus. Emerging evidence, including the coordinated loss of the nuclear lamina (NL) and the histones, supports the involvement of the NL in spermatid nuclear remodelling, but how the NL links to the chromatin is not known. In somatic cells, interactions between the NL and the chromatin have been demonstrated: LEM-domain proteins and LBR interact with the NL and respectively, the chromatin proteins BAF and HP1. We therefore sought to characterise the lamina-chromatin interface during spermiogenesis, by investigating the localisation of six LEM-domain proteins, two BAF proteins and LBR, in human spermatids and spermatozoa. Using RT-PCR, IF and western blotting, we show that six of the proteins tested are present in spermatids: LEMD1, LEMD2 (a short isoform), ANKLE2, LAP2β, BAF and BAF-L, and three absent: Emerin, LBR and LEMD3. The full-length LEMD2 isoform, required for nuclear integrity in somatic cells, is absent. In spermatids, no protein localised to the nuclear periphery, but five were nucleoplasmic, receding towards the posterior nuclear pole as spermatids matured. Our study therefore establishes that the lamina-chromatin interface in human spermatids is radically distinct from that defined in somatic cells. In ejaculated spermatozoa, we detected only BAF and BAF-L, suggesting that they might contribute to the shaping of the spermatozoon nucleus and, after fertilisation, its transition to the male pronucleus. … (more)
- Is Part Of:
- Reproduction. Volume 154:Issue 4(2017)
- Journal:
- Reproduction
- Issue:
- Volume 154:Issue 4(2017)
- Issue Display:
- Volume 154, Issue 4 (2017)
- Year:
- 2017
- Volume:
- 154
- Issue:
- 4
- Issue Sort Value:
- 2017-0154-0004-0000
- Page Start:
- 387
- Page End:
- 401
- Publication Date:
- 2017-10
- Subjects:
- Reproduction -- Periodicals
Reproduction -- Molecular aspects -- Periodicals
Reproduction -- Immunological aspects -- Periodicals
Reproduction -- Endocrine aspects -- Periodicals
Fertility -- Periodicals
Human reproduction -- Periodicals
571.805 - Journal URLs:
- http://www.bioscientifica.com/ ↗
http://www.reproduction-online.org/ ↗
http://www.srf-reproduction.org/journal/ ↗ - DOI:
- 10.1530/REP-17-0358 ↗
- Languages:
- English
- ISSNs:
- 1470-1626
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 11715.xml