Muniscins

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 2 Umasankar PK, Ma L, Thieman JR, Jha A, Doray B, Watkins SC, Traub LM (2014). "A clathrin coat assembly role for the muniscin protein central linker revealed by TALEN-mediated gene editing". eLife. 3. PMC 4215538 Freely accessible. PMID 25303365. doi:10.7554/eLife.04137.
  2. ↑ Shimada A, Yamaguchi A, Kohda D (2016). "Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 μ homology domain". Scientific Reports. 6: 19565. PMC 4731787 Freely accessible. PMID 26822536. doi:10.1038/srep19565.
  3. ↑ Weissenhorn W (2005). "Crystal structure of the endophilin-A1 BAR domain". Journal of Molecular Biology. 351 (3): 653–61. PMID 16023669. doi:10.1016/j.jmb.2005.06.013.
  4. ↑ Reider A, Barker SL, Mishra SK, Im YJ, Maldonado-Báez L, Hurley JH, Traub LM, Wendland B (2009). "Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation". The EMBO Journal. 28 (20): 3103–16. PMC 2771086 Freely accessible. PMID 19713939. doi:10.1038/emboj.2009.248.
  5. 1 2 3 4 Robinson MS (2015). "Forty Years of Clathrin-coated Vesicles". Traffic (Copenhagen, Denmark). 16 (12): 1210–38. PMID 26403691. doi:10.1111/tra.12335.
  6. ↑ anon. "SYP1 [Saccharomyces cerevisiae]". ncbi.nlm.nih.gov/. ncbi.nlm.nih.gov/. Retrieved 26 May 2017.
  7. ↑ Boettner DR, D'Agostino JL, Torres OT, Daugherty-Clarke K, Uygur A, Reider A, Wendland B, Lemmon SK, Goode BL (2009). "The F-BAR protein Syp1 negatively regulates WASp-Arp2/3 complex activity during endocytic patch formation". Current Biology : CB. 19 (23): 1979–87. PMC 2828323 Freely accessible. PMID 19962315. doi:10.1016/j.cub.2009.10.062.
  8. ↑ Dergai O, Novokhatska O, Dergai M, Skrypkina I, Tsyba L, Moreau J, Rynditch A (2010). "Intersectin 1 forms complexes with SGIP1 and Reps1 in clathrin-coated pits". Biochemical and Biophysical Research Communications. 402 (2): 408–13. PMID 20946875. doi:10.1016/j.bbrc.2010.10.045.
  9. ↑ Henne WM, Boucrot E, Meinecke M, Evergren E, Vallis Y, Mittal R, McMahon HT (2010). "FCHo proteins are nucleators of clathrin-mediated endocytosis". Science (New York, N.Y.). 328 (5983): 1281–4. PMC 2883440 Freely accessible. PMID 20448150. doi:10.1126/science.1188462.
  10. ↑ Cocucci E, Aguet F, Boulant S, Kirchhausen T (2012). "The first five seconds in the life of a clathrin-coated pit". Cell. 150 (3): 495–507. PMC 3413093 Freely accessible. PMID 22863004. doi:10.1016/j.cell.2012.05.047.
  11. ↑ Hirst J, Schlacht A, Norcott JP, Traynor D, Bloomfield G, Antrobus R, Kay RR, Dacks JB, Robinson MS (2014). "Characterization of TSET, an ancient and widespread membrane trafficking complex". eLife. 3: e02866. PMC 4031984 Freely accessible. PMID 24867644. doi:10.7554/eLife.02866.
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