Nuclear Envelope Retention of LINC Complexes Is Promoted by SUN-1 Oligomerization in the Caenorhabditis elegans Germ Line.
Genetics
; 203(2): 733-48, 2016 06.
Article
en En
| MEDLINE
| ID: mdl-27098914
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 oligomerization and retention of the protein in the nuclear envelope, especially at later stages of female gametogenesis. Consistently, deletion of the coiled-coil domain makes SUN-1 sensitive to unilateral force exposure across the nuclear membrane. Premature loss of SUN-1 from the nuclear envelope leads to embryonic death due to loss of centrosome-nuclear envelope attachment. However, in contrast to previous notions we can show that the coiled-coil domain is dispensable for functional LINC complex formation, exemplified by successful chromosome sorting and synapsis in meiotic prophase I in its absence.
Palabras clave
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Oogonios
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Caenorhabditis elegans
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Receptores Citoplasmáticos y Nucleares
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Proteínas de Caenorhabditis elegans
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Multimerización de Proteína
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Membrana Nuclear
Límite:
Animals
Idioma:
En
Revista:
Genetics
Año:
2016
Tipo del documento:
Article
País de afiliación:
Austria