Muniscins

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]

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

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. 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. doi:10.7554/eLife.04137. PMC 4215538. PMID 25303365.
  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. doi:10.1038/srep19565. PMC 4731787. PMID 26822536.
  3. Weissenhorn W (2005). "Crystal structure of the endophilin-A1 BAR domain". Journal of Molecular Biology. 351 (3): 653–61. doi:10.1016/j.jmb.2005.06.013. PMID 16023669.
  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. doi:10.1038/emboj.2009.248. PMC 2771086. PMID 19713939.
  5. Robinson MS (2015). "Forty Years of Clathrin-coated Vesicles". Traffic. 16 (12): 1210–38. doi:10.1111/tra.12335. PMID 26403691.
  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. 19 (23): 1979–87. doi:10.1016/j.cub.2009.10.062. PMC 2828323. PMID 19962315.
  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. doi:10.1016/j.bbrc.2010.10.045. PMID 20946875.
  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. 328 (5983): 1281–4. doi:10.1126/science.1188462. PMC 2883440. PMID 20448150.
  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. doi:10.1016/j.cell.2012.05.047. PMC 3413093. PMID 22863004.
  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. doi:10.7554/eLife.02866. PMC 4031984. PMID 24867644.
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