Characterization of a γ-adaptin ear-binding motif in enthoprotin

Enthoprotin, a newly identified component of clathrin-coated vesicles, interacts with the trans-Golgi network (TGN) clathrin adapters AP-1 and GGA2. Here we perform a multi-faceted analysis of the site in enthoprotin that is responsible for the binding to the γ-adaptin ear (γ-ear) domain of AP-1. Al...

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Published inFEBS letters Vol. 555; no. 3; pp. 437 - 442
Main Authors Wasiak, Sylwia, Denisov, Alexei Yu, Han, Zhaozhong, Leventis, Peter A., de Heuvel, Elaine, Boulianne, Gabrielle L., Kay, Brian K., Gehring, Kalle, McPherson, Peter S.
Format Journal Article
LanguageEnglish
Published England Elsevier B.V 18.12.2003
Subjects
Adaptor Protein Complex gamma Subunits - metabolism
Alanine - genetics
Alanine - metabolism
Amino Acid Motifs - genetics
Amino Acid Sequence
Amino Acid Substitution
Animals
AP-1
AP-2
Binding Sites
Cell Line
Clathrin
Clathrin-coated vesicle
Humans
Mice
Models, Molecular
Molecular Sequence Data
NMR, trans-Golgi network
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Alignment
Transcription Factor AP-1 - chemistry
Transcription Factor AP-1 - metabolism
Transfection
Clathrin
AP-2
AP-1
NMR, trans-Golgi network
Clathrin-coated vesicle
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Abstract Enthoprotin, a newly identified component of clathrin-coated vesicles, interacts with the trans-Golgi network (TGN) clathrin adapters AP-1 and GGA2. Here we perform a multi-faceted analysis of the site in enthoprotin that is responsible for the binding to the γ-adaptin ear (γ-ear) domain of AP-1. Alanine scan mutagenesis and nuclear magnetic resonance (NMR) studies reveal the full extent of the site as well as critical residues for this interaction. NMR studies of the γ-ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the γ-ear.
AbstractList Enthoprotin, a newly identified component of clathrin‐coated vesicles, interacts with the trans ‐Golgi network (TGN) clathrin adapters AP‐1 and GGA2. Here we perform a multi‐faceted analysis of the site in enthoprotin that is responsible for the binding to the γ‐adaptin ear (γ‐ear) domain of AP‐1. Alanine scan mutagenesis and nuclear magnetic resonance (NMR) studies reveal the full extent of the site as well as critical residues for this interaction. NMR studies of the γ‐ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the γ‐ear.
Enthoprotin, a newly identified component of clathrin-coated vesicles, interacts with the trans-Golgi network (TGN) clathrin adapters AP-1 and GGA2. Here we perform a multi-faceted analysis of the site in enthoprotin that is responsible for the binding to the γ-adaptin ear (γ-ear) domain of AP-1. Alanine scan mutagenesis and nuclear magnetic resonance (NMR) studies reveal the full extent of the site as well as critical residues for this interaction. NMR studies of the γ-ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the γ-ear.
Enthoprotin, a newly identified component of clathrin‐coated vesicles, interacts with the trans‐Golgi network (TGN) clathrin adapters AP‐1 and GGA2. Here we perform a multi‐faceted analysis of the site in enthoprotin that is responsible for the binding to the γ‐adaptin ear (γ‐ear) domain of AP‐1. Alanine scan mutagenesis and nuclear magnetic resonance (NMR) studies reveal the full extent of the site as well as critical residues for this interaction. NMR studies of the γ‐ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the γ‐ear.
Enthoprotin, a newly identified component of clathrin-coated vesicles, interacts with the trans-Golgi network (TGN) clathrin adapters AP-1 and GGA2. Here we perform a multi-faceted analysis of the site in enthoprotin that is responsible for the binding to the gamma-adaptin ear (gamma-ear) domain of AP-1. Alanine scan mutagenesis and nuclear magnetic resonance (NMR) studies reveal the full extent of the site as well as critical residues for this interaction. NMR studies of the gamma-ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the gamma-ear.
Author Wasiak, Sylwia
Leventis, Peter A.
Denisov, Alexei Yu
Gehring, Kalle
Kay, Brian K.
Boulianne, Gabrielle L.
McPherson, Peter S.
Han, Zhaozhong
de Heuvel, Elaine
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  fullname: McPherson, Peter S.
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FEBS Letters 555 (2003) 1873-3468 © 2015 Federation of European Biochemical Societies
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Keywords Clathrin
AP-2
AP-1
NMR, trans-Golgi network
Clathrin-coated vesicle
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Snippet Enthoprotin, a newly identified component of clathrin-coated vesicles, interacts with the trans-Golgi network (TGN) clathrin adapters AP-1 and GGA2. Here we...
Enthoprotin, a newly identified component of clathrin‐coated vesicles, interacts with the trans‐Golgi network (TGN) clathrin adapters AP‐1 and GGA2. Here we...
Enthoprotin, a newly identified component of clathrin-coated vesicles, interacts with the trans-Golgi network (TGN) clathrin adapters AP-1 and GGA2. Here we...
Enthoprotin, a newly identified component of clathrin‐coated vesicles, interacts with the trans ‐Golgi network (TGN) clathrin adapters AP‐1 and GGA2. Here we...
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wiley
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SubjectTerms Adaptor Protein Complex gamma Subunits - metabolism
Alanine - genetics
Alanine - metabolism
Amino Acid Motifs - genetics
Amino Acid Sequence
Amino Acid Substitution
Animals
AP-1
AP-2
Binding Sites
Cell Line
Clathrin
Clathrin-coated vesicle
Humans
Mice
Models, Molecular
Molecular Sequence Data
NMR, trans-Golgi network
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - metabolism
Sequence Alignment
Transcription Factor AP-1 - chemistry
Transcription Factor AP-1 - metabolism
Transfection
Title Characterization of a γ-adaptin ear-binding motif in enthoprotin
URI https://dx.doi.org/10.1016/S0014-5793(03)01299-7
https://onlinelibrary.wiley.com/doi/abs/10.1016%2FS0014-5793%2803%2901299-7
https://www.ncbi.nlm.nih.gov/pubmed/14675752
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