Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins

Michael D Healy; Joanna Sacharz; Kerrie E McNally; Calum McConville; Vikas A Tillu; Ryan J Hall; Molly Chilton; Peter J Cullen; Mehdi Mobli; Rajesh Ghai; David A Stroud; Brett M Collins

doi:10.1016/j.str.2022.10.001

Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins

Michael D Healy, Joanna Sacharz, Kerrie E McNally, Calum McConville, Vikas A Tillu, Ryan J Hall, Molly Chilton, Peter J Cullen, Mehdi Mobli, Rajesh Ghai, David A Stroud, Brett M Collins

Research output: Contribution to journal › Article (Academic Journal) › peer-review

9 Citations (Scopus)

Abstract

The sorting nexin SNX17 controls endosomal recycling of transmembrane cargo proteins including integrins, the amyloid precursor protein, and lipoprotein receptors. This requires association with the Commander trafficking complex and depends on the C terminus of SNX17 through unknown mechanisms. Using proteomics, we find that the SNX17 C terminus is sufficient for Commander interaction and also associates with members of the PDZ and LIM domain (PDLIM) family. SNX17 contains a type III PDZ binding motif that binds specifically to the PDLIM proteins. The structure of the PDLIM7 PDZ domain bound to the SNX17 C terminus reveals an unconventional perpendicular peptide interaction mediated by electrostatic contacts and a uniquely conserved proline-containing loop sequence in the PDLIM protein family. Our results define the mechanism of SNX17-PDLIM interaction and suggest that the PDLIM proteins may play a role in regulating the activity of SNX17 in conjunction with Commander and actin-rich endosomal trafficking domains.

Original language	English
Pages (from-to)	1590-1602
Number of pages	13
Journal	Structure
Volume	30
Issue number	12
Early online date	18 Oct 2022
DOIs	https://doi.org/10.1016/j.str.2022.10.001
Publication status	E-pub ahead of print - 18 Oct 2022

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Publisher Copyright:
Copyright © 2022. Published by Elsevier Ltd.

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Healy, M. D., Sacharz, J., McNally, K. E., McConville, C., Tillu, V. A., Hall, R. J., Chilton, M., Cullen, P. J., Mobli, M., Ghai, R., Stroud, D. A., & Collins, B. M. (2022). Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins. Structure, 30(12), 1590-1602. Advance online publication. https://doi.org/10.1016/j.str.2022.10.001

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title = "Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins",

abstract = "The sorting nexin SNX17 controls endosomal recycling of transmembrane cargo proteins including integrins, the amyloid precursor protein, and lipoprotein receptors. This requires association with the Commander trafficking complex and depends on the C terminus of SNX17 through unknown mechanisms. Using proteomics, we find that the SNX17 C terminus is sufficient for Commander interaction and also associates with members of the PDZ and LIM domain (PDLIM) family. SNX17 contains a type III PDZ binding motif that binds specifically to the PDLIM proteins. The structure of the PDLIM7 PDZ domain bound to the SNX17 C terminus reveals an unconventional perpendicular peptide interaction mediated by electrostatic contacts and a uniquely conserved proline-containing loop sequence in the PDLIM protein family. Our results define the mechanism of SNX17-PDLIM interaction and suggest that the PDLIM proteins may play a role in regulating the activity of SNX17 in conjunction with Commander and actin-rich endosomal trafficking domains.",

author = "Healy, {Michael D} and Joanna Sacharz and McNally, {Kerrie E} and Calum McConville and Tillu, {Vikas A} and Hall, {Ryan J} and Molly Chilton and Cullen, {Peter J} and Mehdi Mobli and Rajesh Ghai and Stroud, {David A} and Collins, {Brett M}",

note = "Publisher Copyright: Copyright {\textcopyright} 2022. Published by Elsevier Ltd.",

year = "2022",

month = oct,

day = "18",

doi = "10.1016/j.str.2022.10.001",

language = "English",

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T1 - Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins

AU - Healy, Michael D

AU - Sacharz, Joanna

AU - McNally, Kerrie E

AU - McConville, Calum

AU - Tillu, Vikas A

AU - Hall, Ryan J

AU - Chilton, Molly

AU - Cullen, Peter J

AU - Mobli, Mehdi

AU - Ghai, Rajesh

AU - Stroud, David A

AU - Collins, Brett M

PY - 2022/10/18

Y1 - 2022/10/18

N2 - The sorting nexin SNX17 controls endosomal recycling of transmembrane cargo proteins including integrins, the amyloid precursor protein, and lipoprotein receptors. This requires association with the Commander trafficking complex and depends on the C terminus of SNX17 through unknown mechanisms. Using proteomics, we find that the SNX17 C terminus is sufficient for Commander interaction and also associates with members of the PDZ and LIM domain (PDLIM) family. SNX17 contains a type III PDZ binding motif that binds specifically to the PDLIM proteins. The structure of the PDLIM7 PDZ domain bound to the SNX17 C terminus reveals an unconventional perpendicular peptide interaction mediated by electrostatic contacts and a uniquely conserved proline-containing loop sequence in the PDLIM protein family. Our results define the mechanism of SNX17-PDLIM interaction and suggest that the PDLIM proteins may play a role in regulating the activity of SNX17 in conjunction with Commander and actin-rich endosomal trafficking domains.

AB - The sorting nexin SNX17 controls endosomal recycling of transmembrane cargo proteins including integrins, the amyloid precursor protein, and lipoprotein receptors. This requires association with the Commander trafficking complex and depends on the C terminus of SNX17 through unknown mechanisms. Using proteomics, we find that the SNX17 C terminus is sufficient for Commander interaction and also associates with members of the PDZ and LIM domain (PDLIM) family. SNX17 contains a type III PDZ binding motif that binds specifically to the PDLIM proteins. The structure of the PDLIM7 PDZ domain bound to the SNX17 C terminus reveals an unconventional perpendicular peptide interaction mediated by electrostatic contacts and a uniquely conserved proline-containing loop sequence in the PDLIM protein family. Our results define the mechanism of SNX17-PDLIM interaction and suggest that the PDLIM proteins may play a role in regulating the activity of SNX17 in conjunction with Commander and actin-rich endosomal trafficking domains.

U2 - 10.1016/j.str.2022.10.001

DO - 10.1016/j.str.2022.10.001

M3 - Article (Academic Journal)

C2 - 36302387

SN - 0969-2126

VL - 30

SP - 1590

EP - 1602

JO - Structure

JF - Structure

IS - 12

ER -

Proteomic identification and structural basis for the interaction between sorting nexin SNX17 and PDLIM family proteins

Abstract

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