Accessory protein recruitment motifs in clathrin-mediated endocytosis

Tom J. Brett; Linton M. Traub; Daved H. Fremont

doi:10.1016/S0969-2126(02)00784-0

Accessory protein recruitment motifs in clathrin-mediated endocytosis

Tom J. Brett, Linton M. Traub, Daved H. Fremont

Research output: Contribution to journal › Article › peer-review

167 Scopus citations

Abstract

Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the α-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I β turn conformations to a conserved pocket on the α-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.

Original language	English
Pages (from-to)	797-809
Number of pages	13
Journal	Structure
Volume	10
Issue number	6
DOIs	https://doi.org/10.1016/S0969-2126(02)00784-0
State	Published - 2002

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@article{95deb385295f48a687db6ab3f792b7c7,

title = "Accessory protein recruitment motifs in clathrin-mediated endocytosis",

abstract = "Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the α-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I β turn conformations to a conserved pocket on the α-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.",

author = "Brett, {Tom J.} and Traub, {Linton M.} and Fremont, {Daved H.}",

note = "Funding Information: We thank Rainer K. Brachmann, Chris Nelson, Andrey S. Shaw, and Gabriel Waksman for critical comments on the manuscript. We thank Paul M. Allen for peptide synthesis and discussions. This work was funded in part by grants from the Barnes-Jewish Foundation, the Burroughs-Wellcome Fund, and NIH. ",

year = "2002",

doi = "10.1016/S0969-2126(02)00784-0",

language = "English",

volume = "10",

pages = "797--809",

journal = "Structure",

issn = "0969-2126",

number = "6",

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T1 - Accessory protein recruitment motifs in clathrin-mediated endocytosis

AU - Brett, Tom J.

AU - Traub, Linton M.

AU - Fremont, Daved H.

N1 - Funding Information: We thank Rainer K. Brachmann, Chris Nelson, Andrey S. Shaw, and Gabriel Waksman for critical comments on the manuscript. We thank Paul M. Allen for peptide synthesis and discussions. This work was funded in part by grants from the Barnes-Jewish Foundation, the Burroughs-Wellcome Fund, and NIH.

PY - 2002

Y1 - 2002

N2 - Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the α-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I β turn conformations to a conserved pocket on the α-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.

AB - Clathrin-mediated endocytosis depends upon the interaction of accessory proteins with the α-ear of the AP-2 adaptor. We present structural characterization of these regulatory interactions. DPF and DPW motif peptides derived from eps15 and epsin bind in type I β turn conformations to a conserved pocket on the α-ear platform. We show evidence for a second binding site that is DPW motif specific. The structure of a complex with an AP-2 binding segment from amphiphysin reveals a novel binding motif that we term FxDxF, which is engaged in an extended conformation by a unique surface of the platform domain. The FxDxF motif is also used by AP180 and the 170 kDa isoform of synaptojanin and can be found in several potential endocytic proteins, including HIP1, CD2AP, and PLAP. A mechanism of clathrin assembly regulation is suggested by three different AP-2 engagement modes.

UR - http://www.scopus.com/inward/record.url?scp=0036278105&partnerID=8YFLogxK

U2 - 10.1016/S0969-2126(02)00784-0

DO - 10.1016/S0969-2126(02)00784-0

M3 - Article

C2 - 12057195

AN - SCOPUS:0036278105

SN - 0969-2126

VL - 10

SP - 797

EP - 809

JO - Structure

JF - Structure

IS - 6

ER -

Accessory protein recruitment motifs in clathrin-mediated endocytosis

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