Unknown

Dataset Information

0

Expression of individual mammalian Sun1 isoforms depends on the cell type.


ABSTRACT: Mammalian Sun1 belongs to an evolutionarily conserved family of inner nuclear membrane proteins, which are known as SUN domain proteins. SUN domain proteins interact with KASH domain partners to form bridging complexes, so-called LINC complexes, that physically connect the nuclear interior to the cytoskeleton. LINC complexes are critical for nuclear integrity and play fundamental roles in nuclear positioning, shaping and movement. The mammalian genome codes for at least five different SUN domain proteins used for the formation of a number of different LINC complexes. Recently, we reported on the identification of several Sun1 isoforms, which tremendously enlarges the alternatives to form functional LINC complexes. We now confirmed that Sun1 actually exists in at least seven distinct splice variants. Besides that, we observed that expression of individual Sun1 isoforms remarkably depends on the cell type, suggesting a cell type-specific adaption of Sun1 dependent LINC complexes to specific cellular and physiological requirements.

SUBMITTER: Gob E 

PROVIDER: S-EPMC3181515 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

altmetric image

Publications

Expression of individual mammalian Sun1 isoforms depends on the cell type.

Göb Eva E   Meyer-Natus Elisabeth E   Benavente Ricardo R   Alsheimer Manfred M  

Communicative & integrative biology 20110701 4


Mammalian Sun1 belongs to an evolutionarily conserved family of inner nuclear membrane proteins, which are known as SUN domain proteins. SUN domain proteins interact with KASH domain partners to form bridging complexes, so-called LINC complexes, that physically connect the nuclear interior to the cytoskeleton. LINC complexes are critical for nuclear integrity and play fundamental roles in nuclear positioning, shaping and movement. The mammalian genome codes for at least five different SUN domain  ...[more]

Similar Datasets

| S-EPMC4733560 | biostudies-literature
| S-EPMC6853637 | biostudies-literature
| S-EPMC4787764 | biostudies-literature
| S-EPMC3410425 | biostudies-literature
| S-EPMC7074989 | biostudies-literature
| S-EPMC8479664 | biostudies-literature
| S-EPMC2802713 | biostudies-literature
| S-EPMC10778272 | biostudies-literature
| S-EPMC4426136 | biostudies-literature
| S-EPMC6295722 | biostudies-literature