PMID- 28357352
OWN - NLM
STAT- PubMed-not-MEDLINE
LR  - 20201001
IS  - 2311-2638 (Print)
IS  - 2311-2638 (Electronic)
IS  - 2311-2638 (Linking)
VI  - 3
IP  - 4
DP  - 2016 Apr 4
TI  - Chromatin binding and silencing: Two roles of the same protein Lem2.
PG  - 185-188
LID - 10.15698/mic2016.04.495 [doi]
AB  - Transcriptionally repressed chromatin localizes to specific areas within the 
      eukaryotic nucleus and is often found at the nuclear periphery, which is thought 
      to provide a specialized compartment for gene silencing. However, the molecular 
      mechanisms that establish this spatial chromatin organization are still poorly 
      understood. In our recent work (Barrales et al. 2016), we identified the nuclear 
      envelope protein Lem2, a homolog of metazoan lamin-associated proteins (LAPs), as 
      a relevant factor for heterochromatin silencing and perinuclear localization in 
      the fission yeast Schizosaccharomyces pombe. Several other LAPs have previously 
      been reported to associate with heterochromatin, and it has been proposed that 
      this interaction might directly contribute to gene repression, perhaps through 
      tethering via chromatin-binding domains like the LEM domain. We demonstrated that 
      the LEM domain of Lem2 is indeed essential for centromere binding and perinuclear 
      tethering. However, we made the surprising finding that tethering via the LEM 
      domain is functionally independent of Lem2's role in silencing, which instead is 
      mediated by a different part of the protein, the MSC domain. Our study 
      demonstrates that tethering and silencing, although mediated by the same 
      molecule, Lem2, can be mechanistically separated. This further unveils a complex 
      function of this protein at the interface between the nuclear periphery and 
      silent chromatin, which might be preserved among the other members of this 
      conserved family of LEM proteins.
FAU - Barrales, Ramon Ramos
AU  - Barrales RR
AD  - Department of Physiological Chemistry, Biomedical Center, 
      Ludwig-Maximilians-University of Munich, Grosshaderner Str. 9, 82152 Martinsried, 
      Germany.
FAU - Braun, Sigurd
AU  - Braun S
AD  - Department of Physiological Chemistry, Biomedical Center, 
      Ludwig-Maximilians-University of Munich, Grosshaderner Str. 9, 82152 Martinsried, 
      Germany.
LA  - eng
PT  - Comment
PT  - Journal Article
DEP - 20160404
PL  - Austria
TA  - Microb Cell
JT  - Microbial cell (Graz, Austria)
JID - 101632887
CON - Genes Dev. 2016 Jan 15;30(2):133-48. PMID: 26744419
PMC - PMC5349094
OTO - NOTNLM
OT  - LEM
OT  - heterochromatin
OT  - lamin-associated proteins
OT  - perinuclear silencing
OT  - tethering
COIS- Conflict of interest: The authors declare no competing financial interests.
EDAT- 2017/03/31 06:00
MHDA- 2017/03/31 06:01
PMCR- 2016/04/04
CRDT- 2017/03/31 06:00
PHST- 2017/03/31 06:00 [entrez]
PHST- 2017/03/31 06:00 [pubmed]
PHST- 2017/03/31 06:01 [medline]
PHST- 2016/04/04 00:00 [pmc-release]
AID - MIC0176E148 [pii]
AID - 10.15698/mic2016.04.495 [doi]
PST - epublish
SO  - Microb Cell. 2016 Apr 4;3(4):185-188. doi: 10.15698/mic2016.04.495.