PMID- 26048141
OWN - NLM
STAT- MEDLINE
DCOM- 20151125
LR  - 20181113
IS  - 1530-6860 (Electronic)
IS  - 0892-6638 (Print)
IS  - 0892-6638 (Linking)
VI  - 29
IP  - 9
DP  - 2015 Sep
TI  - Actin-bundling protein plastin 3 is a regulator of ectoplasmic specialization 
      dynamics during spermatogenesis in the rat testis.
PG  - 3788-805
LID - 10.1096/fj.14-267997 [doi]
AB  - Ectoplasmic specialization (ES) is an actin-rich adherens junction in the 
      seminiferous epithelium of adult mammalian testes. ES is restricted to the 
      Sertoli-spermatid (apical ES) interface, as well as the Sertoli cell-cell (basal 
      ES) interface at the blood-testis barrier (BTB). ES is typified by the presence 
      of an array of bundles of actin microfilaments near the Sertoli cell plasma 
      membrane. These actin microfilament bundles require rapid debundling to convert 
      them from a bundled to branched/unbundled configuration and vice versa to confer 
      plasticity to support the transport of 1) spermatids in the adluminal compartment 
      and 2) preleptotene spermatocytes at the BTB while maintaining cell adhesion. 
      Plastin 3 is one of the plastin family members abundantly found in yeast, plant 
      and animal cells that confers actin microfilaments their bundled configuration. 
      Herein, plastin 3 was shown to be a component of the apical and basal ES in the 
      rat testis, displaying spatiotemporal expression during the epithelial cycle. A 
      knockdown (KD) of plastin 3 in Sertoli cells by RNA interference using an in 
      vitro model to study BTB function showed that a transient loss of plastin 3 
      perturbed the Sertoli cell tight junction-permeability barrier, mediated by 
      changes in the localization of basal ES proteins N-cadherin and beta-catenin. More 
      importantly, these changes were the result of an alteration of the actin 
      microfilaments, converting from their bundled to branched configuration when 
      examined microscopically, and validated by biochemical assays that quantified 
      actin-bundling and polymerization activity. Moreover, these changes were 
      confirmed by studies in vivo by plastin 3 KD in the testis in which 
      mis-localization of N-cadherin and beta-catenin was also detected at the BTB, 
      concomitant with defects in the transport of spermatids and phagosomes and a 
      disruption of cell adhesion most notably in elongated spermatids due to a loss of 
      actin-bundling capability at the apical ES, which in turn affected localization 
      of adhesion protein complexes at the site. In summary, plastin 3 is a regulator 
      of actin microfilament bundles at the ES in which it dictates the configuration 
      of the filamentous actin network by assuming either a bundled or 
      unbundled/branched configuration via changes in its spatiotemporal expression 
      during the epithelial cycle.
CI  - (c) FASEB.
FAU - Li, Nan
AU  - Li N
AD  - *The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for 
      Biomedical Research, Population Council, New York, New York, USA; Department of 
      Biology, Hong Kong Baptist University, Hong Kong, China; School of Biological 
      Sciences, University of Hong Kong, Hong Kong, China; and Institute of Basic 
      Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, 
      Peking Union Medical College, Beijing, China.
FAU - Mruk, Dolores D
AU  - Mruk DD
AD  - *The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for 
      Biomedical Research, Population Council, New York, New York, USA; Department of 
      Biology, Hong Kong Baptist University, Hong Kong, China; School of Biological 
      Sciences, University of Hong Kong, Hong Kong, China; and Institute of Basic 
      Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, 
      Peking Union Medical College, Beijing, China.
FAU - Wong, Chris K C
AU  - Wong CK
AD  - *The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for 
      Biomedical Research, Population Council, New York, New York, USA; Department of 
      Biology, Hong Kong Baptist University, Hong Kong, China; School of Biological 
      Sciences, University of Hong Kong, Hong Kong, China; and Institute of Basic 
      Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, 
      Peking Union Medical College, Beijing, China.
FAU - Lee, Will M
AU  - Lee WM
AD  - *The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for 
      Biomedical Research, Population Council, New York, New York, USA; Department of 
      Biology, Hong Kong Baptist University, Hong Kong, China; School of Biological 
      Sciences, University of Hong Kong, Hong Kong, China; and Institute of Basic 
      Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, 
      Peking Union Medical College, Beijing, China.
FAU - Han, Daishu
AU  - Han D
AD  - *The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for 
      Biomedical Research, Population Council, New York, New York, USA; Department of 
      Biology, Hong Kong Baptist University, Hong Kong, China; School of Biological 
      Sciences, University of Hong Kong, Hong Kong, China; and Institute of Basic 
      Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, 
      Peking Union Medical College, Beijing, China.
FAU - Cheng, C Yan
AU  - Cheng CY
AD  - *The Mary M. Wohlford Laboratory for Male Contraceptive Research, Center for 
      Biomedical Research, Population Council, New York, New York, USA; Department of 
      Biology, Hong Kong Baptist University, Hong Kong, China; School of Biological 
      Sciences, University of Hong Kong, Hong Kong, China; and Institute of Basic 
      Medical Sciences, Chinese Academy of Medical Sciences, School of Basic Medicine, 
      Peking Union Medical College, Beijing, China y-cheng@popcbr.rockefeller.edu.
LA  - eng
GR  - R01 HD056034/HD/NICHD NIH HHS/United States
GR  - U54 HD029990/HD/NICHD NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20150605
PL  - United States
TA  - FASEB J
JT  - FASEB journal : official publication of the Federation of American Societies for 
      Experimental Biology
JID - 8804484
RN  - 0 (Cadherins)
RN  - 0 (Membrane Glycoproteins)
RN  - 0 (Microfilament Proteins)
RN  - 0 (N-cadherin, rat)
RN  - 0 (Nerve Tissue Proteins)
RN  - 0 (beta Catenin)
RN  - 0 (plastin)
SB  - IM
MH  - Actin Cytoskeleton/metabolism
MH  - Animals
MH  - Cadherins/metabolism
MH  - Male
MH  - Membrane Glycoproteins/*metabolism
MH  - Microfilament Proteins/*metabolism
MH  - Nerve Tissue Proteins/metabolism
MH  - Rats
MH  - Rats, Sprague-Dawley
MH  - Sertoli Cells/cytology/*metabolism
MH  - Spermatids/cytology/*metabolism
MH  - Spermatocytes/cytology/*metabolism
MH  - Spermatogenesis/*physiology
MH  - Tight Junctions/*metabolism
MH  - beta Catenin/metabolism
PMC - PMC4550371
OTO - NOTNLM
OT  - actin microfilaments
OT  - blood-testis barrier
OT  - spermatid adhesion
EDAT- 2015/06/07 06:00
MHDA- 2015/12/15 06:00
PMCR- 2016/09/01
CRDT- 2015/06/07 06:00
PHST- 2015/01/07 00:00 [received]
PHST- 2015/05/18 00:00 [accepted]
PHST- 2015/06/07 06:00 [entrez]
PHST- 2015/06/07 06:00 [pubmed]
PHST- 2015/12/15 06:00 [medline]
PHST- 2016/09/01 00:00 [pmc-release]
AID - fj.14-267997 [pii]
AID - FJ_267997 [pii]
AID - 10.1096/fj.14-267997 [doi]
PST - ppublish
SO  - FASEB J. 2015 Sep;29(9):3788-805. doi: 10.1096/fj.14-267997. Epub 2015 Jun 5.