Biology:SUN domain

From HandWiki
Sad1_UNC
Identifiers
SymbolSad1_UNC
PfamPF07738
Pfam clanCL0202
InterProIPR012919

SUN (Sad1p, UNC-84) domains are conserved C-terminal protein regions a few hundred amino acids long. SUN domains are usually found following a transmembrane domain and a less conserved region of amino acids. Most proteins containing SUN domains are thought to be involved in the positioning of the nucleus in the cell. It is thought that SUN domains interact directly with KASH domains in the space between the outer and inner nuclear membranes to bridge the nuclear envelope and transfer force from the nucleoskeleton to the cytoplasmic cytoskeleton which enables mechanosensory roles in cells.[1] SUN proteins are thought to localize to the inner nuclear membrane.[2] The S. pombe Sad1 protein localises at the spindle pole body. In mammals, the SUN domain is present in two proteins, Sun1 and Sun2. The SUN domain of Sun2 has been demonstrated to be in the periplasm.[3][4]

Examples of SUN proteins

Caenorhabditis elegans

  • SUN-1/matefin
  • UNC-84

Drosophila melanogaster

  • Klaroid
  • Spag4

Mammals

  • SUN1, SUN2, SUN3, SUN4, SUN5

Schizosaccharomyces pombe

  • Sad1p

Saccharomyces cerevisiae

  • Mps3p

Maize

  • SUN1, SUN2, SUN3, SUN4, SUN5

Arabidopsis

  • SUN1, SUN2

References

  1. "Cell Mechanosensitivity to Extremely Low-Magnitude Signals Is Enabled by a LINCed Nucleus". Stem Cells 33 (6): 2063–76. June 2015. doi:10.1002/stem.2004. PMID 25787126. 
  2. "SUN-domain proteins: 'Velcro' that links the nucleoskeleton to the cytoskeleton". Nature Reviews. Molecular Cell Biology 7 (10): 782–8. October 2006. doi:10.1038/nrm2003. PMID 16926857. https://zenodo.org/record/999029. 
  3. "Sun2 is a novel mammalian inner nuclear membrane protein". The Journal of Biological Chemistry 279 (24): 25805–12. June 2004. doi:10.1074/jbc.M313157200. PMID 15082709. 
  4. "The missing (L) UNC?". Current Biology 9 (18): R708-10. September 1999. doi:10.1016/S0960-9822(99)80446-1. PMID 10508607. 
This article incorporates text from the public domain Pfam and InterPro: IPR012919