2016
DOI: 10.1534/genetics.116.188094
|View full text |Cite
|
Sign up to set email alerts
|

Nuclear Envelope Retention of LINC Complexes Is Promoted by SUN-1 Oligomerization in the Caenorhabditis elegans Germ Line

Abstract: SUN (Sad1 and UNC-84) and KASH (Klarsicht, ANC-1, and Syne homology) proteins are constituents of the inner and outer nuclear membranes. They interact in the perinuclear space via C-terminal SUN-KASH domains to form the linker of nucleoskeleton and cytoskeleton (LINC) complex thereby bridging the nuclear envelope. LINC complexes mediate numerous biological processes by connecting chromatin with the cytoplasmic force-generating machinery. Here we show that the coiled-coil domains of SUN-1 are required for oligo… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1
1
1
1

Citation Types

0
5
0

Year Published

2016
2016
2021
2021

Publication Types

Select...
6
1

Relationship

0
7

Authors

Journals

citations
Cited by 8 publications
(5 citation statements)
references
References 66 publications
(107 reference statements)
0
5
0
Order By: Relevance
“…Finally, we cannot overlook the possibility of different mechanisms of LINC formation and function across organisms. For example, contrary to all published data on human and mouse LINC complexes, Daryabeigi et al (64) recently showed that in Caenorhabditis elegans, the oligomerization of SUN1 is not required for the formation of a functional LINC complex. It would be interesting to see how altered oligomerization states could relate to the diverse functions of these highly conserved SUN domain proteins across organisms (65).…”
Section: Autoinhibition Of the Kash Lid In Sun1mentioning
confidence: 75%
“…Finally, we cannot overlook the possibility of different mechanisms of LINC formation and function across organisms. For example, contrary to all published data on human and mouse LINC complexes, Daryabeigi et al (64) recently showed that in Caenorhabditis elegans, the oligomerization of SUN1 is not required for the formation of a functional LINC complex. It would be interesting to see how altered oligomerization states could relate to the diverse functions of these highly conserved SUN domain proteins across organisms (65).…”
Section: Autoinhibition Of the Kash Lid In Sun1mentioning
confidence: 75%
“…Using the subcellular localization of UAD-2 and the USTC complex as reporters, we have searched for factors that are engaged in H3K27me3-marked facultative heterochromatin compaction and subnuclear localization. SUN-1 is an inner nuclear membrane adaptor protein and is essential for centrosome localization (67). Our candidate-based RNAi screening identified SUN-1, suggesting that SUN-1 may play key roles in recruiting UAD-2 and the USTC complex or heterochromatin to the inner nuclear membrane to create the proper chromatin environment for piRNA transcription.…”
Section: Discussionmentioning
confidence: 93%
“…Accumulation of ZYG-12 at the ONM requires ZYG-12's KASH domain and SUN-1, which together form a relatively immobile complex in the NE (Minn et al 2009). Moreover, oligomerization of SUN-1 (Figure 15; see also Sosa et al 2012) via its central coiled-coil domains contribute to the retention of SUN-1 in the INM, although SUN-1 lacking the coiled-coil domains still form functional LINC complexes (Daryabeigi et al 2016).…”
Section: Pairing Of Meiotic Chromosomesmentioning
confidence: 99%