Epsin N-terminal homology domains bind on opposite sides of two SNAREs
Wang J, Gossing M, Fang P, Zimmermann J, Li X, Fischer von Mollard G, Niu L, Teng M (2011)
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108(30): 12277-12282.
Zeitschriftenaufsatz
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Autor*in
Wang, Jing;
Gossing, MichaelUniBi;
Fang, Pengfei;
Zimmermann, JanaUniBi;
Li, Xu;
Fischer von Mollard, GabrieleUniBi ;
Niu, Liwen;
Teng, Maikun
Einrichtung
Abstract / Bemerkung
SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An opposite surface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid, in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1p in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.
Erscheinungsjahr
2011
Zeitschriftentitel
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Band
108
Ausgabe
30
Seite(n)
12277-12282
ISSN
0027-8424
eISSN
1091-6490
Page URI
https://pub.uni-bielefeld.de/record/2374284
Zitieren
Wang J, Gossing M, Fang P, et al. Epsin N-terminal homology domains bind on opposite sides of two SNAREs. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 2011;108(30):12277-12282.
Wang, J., Gossing, M., Fang, P., Zimmermann, J., Li, X., Fischer von Mollard, G., Niu, L., et al. (2011). Epsin N-terminal homology domains bind on opposite sides of two SNAREs. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(30), 12277-12282. https://doi.org/10.1073/pnas.1013101108
Wang, Jing, Gossing, Michael, Fang, Pengfei, Zimmermann, Jana, Li, Xu, Fischer von Mollard, Gabriele, Niu, Liwen, and Teng, Maikun. 2011. “Epsin N-terminal homology domains bind on opposite sides of two SNAREs”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108 (30): 12277-12282.
Wang, J., Gossing, M., Fang, P., Zimmermann, J., Li, X., Fischer von Mollard, G., Niu, L., and Teng, M. (2011). Epsin N-terminal homology domains bind on opposite sides of two SNAREs. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108, 12277-12282.
Wang, J., et al., 2011. Epsin N-terminal homology domains bind on opposite sides of two SNAREs. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 108(30), p 12277-12282.
J. Wang, et al., “Epsin N-terminal homology domains bind on opposite sides of two SNAREs”, PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, vol. 108, 2011, pp. 12277-12282.
Wang, J., Gossing, M., Fang, P., Zimmermann, J., Li, X., Fischer von Mollard, G., Niu, L., Teng, M.: Epsin N-terminal homology domains bind on opposite sides of two SNAREs. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA. 108, 12277-12282 (2011).
Wang, Jing, Gossing, Michael, Fang, Pengfei, Zimmermann, Jana, Li, Xu, Fischer von Mollard, Gabriele, Niu, Liwen, and Teng, Maikun. “Epsin N-terminal homology domains bind on opposite sides of two SNAREs”. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA 108.30 (2011): 12277-12282.
Daten bereitgestellt von European Bioinformatics Institute (EBI)
UNIPROT
4 Einträge gefunden, die diesen Artikel zitieren
Epsin-3 (UNIPROT: P47160)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Epsin-3 (UNIPROT: P47160)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
t-SNARE VTI1 (UNIPROT: Q04338)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
t-SNARE VTI1 (UNIPROT: Q04338)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Download in FASTA format
PDB
3 Einträge gefunden, die diesen Artikel zitieren
x-ray diffraction (PDB: 3onk)
Protein structure name: yeast ent3_enth domain
Public wwPDB file in PDB format
Protein structure name: yeast ent3_enth domain
Public wwPDB file in PDB format
x-ray diffraction (PDB: 3onj)
Protein structure name: crystal structure of yeast vti1p_habc domain
Public wwPDB file in PDB format
Protein structure name: crystal structure of yeast vti1p_habc domain
Public wwPDB file in PDB format
x-ray diffraction (PDB: 3onl)
Protein structure name: yeast ent3_enth-vti1p_habc complex structure
Public wwPDB file in PDB format
Protein structure name: yeast ent3_enth-vti1p_habc complex structure
Public wwPDB file in PDB format
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