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Title: Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation

Abstract

Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding {mu} homology domains ({mu}HDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The {mu}HD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis.

Authors:
; ; ; ; ; ; ;
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1006195
Resource Type:
Journal Article
Journal Name:
EMBO J.
Additional Journal Information:
Journal Volume: 28; Journal Issue: 2009; Journal ID: ISSN 0261-4189
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 99 GENERAL AND MISCELLANEOUS//MATHEMATICS, COMPUTING, AND INFORMATION SCIENCE; CARGO; IN VITRO; IN VIVO; MEMBRANES; PLASMA; PROTEINS; YEASTS

Citation Formats

Reider, Amanda, Barker, Sarah L, Mishra, Sanjay K, Im, Young Jun, Maldonado-Báez, Lymarie, Hurley, James H, Traub, Linton M, Wendland, Beverly, Pitt), NIH), and JHU). Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. United States: N. p., 2010. Web. doi:10.1038/emboj.2009.248.
Reider, Amanda, Barker, Sarah L, Mishra, Sanjay K, Im, Young Jun, Maldonado-Báez, Lymarie, Hurley, James H, Traub, Linton M, Wendland, Beverly, Pitt), NIH), & JHU). Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation. United States. https://doi.org/10.1038/emboj.2009.248
Reider, Amanda, Barker, Sarah L, Mishra, Sanjay K, Im, Young Jun, Maldonado-Báez, Lymarie, Hurley, James H, Traub, Linton M, Wendland, Beverly, Pitt), NIH), and JHU). 2010. "Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation". United States. https://doi.org/10.1038/emboj.2009.248.
@article{osti_1006195,
title = {Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation},
author = {Reider, Amanda and Barker, Sarah L and Mishra, Sanjay K and Im, Young Jun and Maldonado-Báez, Lymarie and Hurley, James H and Traub, Linton M and Wendland, Beverly and Pitt) and NIH) and JHU)},
abstractNote = {Internalization of diverse transmembrane cargos from the plasma membrane requires a similarly diverse array of specialized adaptors, yet only a few adaptors have been characterized. We report the identification of the muniscin family of endocytic adaptors that is conserved from yeast to human beings. Solving the structures of yeast muniscin domains confirmed the unique combination of an N-terminal domain homologous to the crescent-shaped membrane-tubulating EFC/F-BAR domains and a C-terminal domain homologous to cargo-binding {mu} homology domains ({mu}HDs). In vitro and in vivo assays confirmed membrane-tubulation activity for muniscin EFC/F-BAR domains. The {mu}HD domain has conserved interactions with the endocytic adaptor/scaffold Ede1/eps15, which influences muniscin localization. The transmembrane protein Mid2, earlier implicated in polarized Rho1 signalling, was identified as a cargo of the yeast adaptor protein. These and other data suggest a model in which the muniscins provide a combined adaptor/membrane-tubulation activity that is important for regulating endocytosis.},
doi = {10.1038/emboj.2009.248},
url = {https://www.osti.gov/biblio/1006195}, journal = {EMBO J.},
issn = {0261-4189},
number = 2009,
volume = 28,
place = {United States},
year = {2010},
month = {10}
}