Biology:Muniscins

From HandWiki
Structure of Muniscin proteins[1] and a dimer[2] of FCHO proteins
Ribbon representation of BAR domains from two monomers of endophilin-A1.[3]
The μ homology domain of muniscins evolved from TCUP

The muniscin protein family was initially defined in 2009[4] as proteins having 2 homologous domains that are involved in clathrin mediated endocytosis (CME) and have been reviewed.[5] In addition to FCHO1, FCHO2 and Syp1,[6][7] SGIP1 is also included in the family because it contains the μ (mu) homology domain and is involved in CME, even though it does not contain the F-BAR domain[1][8]

Muniscins are known as alternate cargo adaptors. That is, they participate in selecting which cargo molecules are internalized via CME.[5] Additionally, the structure of the dimer, with its concave face oriented toward the plasma membrane, is thought to help curve the membrane as the clathrin coated pit forms.[5] The muniscins are early arriving proteins involved in CME.[5] FCHO proteins are required for CME,[9] but do not appear to be required to initiate CME.[10]

The μ homology domain of muniscins has been reported to have evolved from part of an ancient cargo adaptor protein complex named TSET.[11]

See also

References

  1. ↑ 1.0 1.1 "A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing". eLife 3. 2014. doi:10.7554/eLife.04137. PMID 25303365. 
  2. ↑ "Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domain". Scientific Reports 6: 19565. 2016. doi:10.1038/srep19565. PMID 26822536. Bibcode: 2016NatSR...619565S. 
  3. ↑ "Crystal structure of the endophilin-A1 BAR domain". Journal of Molecular Biology 351 (3): 653–61. 2005. doi:10.1016/j.jmb.2005.06.013. PMID 16023669. 
  4. ↑ "Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation". The EMBO Journal 28 (20): 3103–16. 2009. doi:10.1038/emboj.2009.248. PMID 19713939. 
  5. ↑ 5.0 5.1 5.2 5.3 "Forty Years of Clathrin-coated Vesicles". Traffic 16 (12): 1210–38. 2015. doi:10.1111/tra.12335. PMID 26403691. https://www.repository.cam.ac.uk/handle/1810/251260. 
  6. ↑ anon. "SYP1 [Saccharomyces cerevisiae"]. https://www.ncbi.nlm.nih.gov/protein/KZV12879.1. 
  7. ↑ "The F-BAR protein Syp1 negatively regulates WASp-Arp2/3 complex activity during endocytic patch formation". Current Biology 19 (23): 1979–87. 2009. doi:10.1016/j.cub.2009.10.062. PMID 19962315. 
  8. ↑ "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits". Biochemical and Biophysical Research Communications 402 (2): 408–13. 2010. doi:10.1016/j.bbrc.2010.10.045. PMID 20946875. 
  9. ↑ "FCHo proteins are nucleators of clathrin-mediated endocytosis". Science 328 (5983): 1281–4. 2010. doi:10.1126/science.1188462. PMID 20448150. Bibcode: 2010Sci...328.1281H. 
  10. ↑ "The first five seconds in the life of a clathrin-coated pit". Cell 150 (3): 495–507. 2012. doi:10.1016/j.cell.2012.05.047. PMID 22863004. 
  11. ↑ "Characterization of TSET, an ancient and widespread membrane trafficking complex". eLife 3: e02866. 2014. doi:10.7554/eLife.02866. PMID 24867644. 



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