Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry

Research output: Contribution to journalJournal articlepeer-review

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Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry. / Jungmichel, Stephanie; Sylvestersen, Kathrine B; Choudhary, Chuna Ram; Nguyen, Steve; Mann, Matthias; Nielsen, Michael L.

In: Cell Reports, Vol. 6, No. 3, 13.02.2014, p. 578-91.

Research output: Contribution to journalJournal articlepeer-review

Harvard

Jungmichel, S, Sylvestersen, KB, Choudhary, CR, Nguyen, S, Mann, M & Nielsen, ML 2014, 'Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry', Cell Reports, vol. 6, no. 3, pp. 578-91. https://doi.org/10.1016/j.celrep.2013.12.038

APA

Jungmichel, S., Sylvestersen, K. B., Choudhary, C. R., Nguyen, S., Mann, M., & Nielsen, M. L. (2014). Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry. Cell Reports, 6(3), 578-91. https://doi.org/10.1016/j.celrep.2013.12.038

Vancouver

Jungmichel S, Sylvestersen KB, Choudhary CR, Nguyen S, Mann M, Nielsen ML. Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry. Cell Reports. 2014 Feb 13;6(3):578-91. https://doi.org/10.1016/j.celrep.2013.12.038

Author

Jungmichel, Stephanie ; Sylvestersen, Kathrine B ; Choudhary, Chuna Ram ; Nguyen, Steve ; Mann, Matthias ; Nielsen, Michael L. / Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry. In: Cell Reports. 2014 ; Vol. 6, No. 3. pp. 578-91.

Bibtex

@article{94c217df2a2c4546b4064f15c4437783,
title = "Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry",
abstract = "Phosphoinositides (PIPs) play key roles in signaling and disease. Using high-resolution quantitative mass spectrometry, we identified PIP-interacting proteins and profiled their binding specificities toward all seven PIP variants. This analysis revealed 405 PIP-binding proteins, which is greater than the total number of phospho- or ubiquitin-binding domains. Translocation and inhibitor assays of identified PIP-binding proteins confirmed that our methodology targets direct interactors. The PIP interactome encompasses proteins from diverse cellular compartments, prominently including the nucleus. Our data set revealed a consensus motif for PI(3,4,5)P3-interacting pleckstrin homology (PH) domains, which enabled in silico identification of phosphoinositide interactors. Members of the dedicator of cytokinesis family C exhibited specificity toward both PI(3,4,5)P3 and PI(4,5)P2. Structurally, this dual specificity is explained by a decreased number of positively charged residues in the L1 subdomain compared with DOCK1. The presented PIP-binding proteome and its specificity toward individual PIPs should be a valuable resource for the community.",
author = "Stephanie Jungmichel and Sylvestersen, {Kathrine B} and Choudhary, {Chuna Ram} and Steve Nguyen and Matthias Mann and Nielsen, {Michael L}",
note = "Copyright {\textcopyright} 2014 The Authors. Published by Elsevier Inc. All rights reserved.",
year = "2014",
month = feb,
day = "13",
doi = "10.1016/j.celrep.2013.12.038",
language = "English",
volume = "6",
pages = "578--91",
journal = "Cell Reports",
issn = "2211-1247",
publisher = "Cell Press",
number = "3",

}

RIS

TY - JOUR

T1 - Specificity and commonality of the phosphoinositide-binding proteome analyzed by quantitative mass spectrometry

AU - Jungmichel, Stephanie

AU - Sylvestersen, Kathrine B

AU - Choudhary, Chuna Ram

AU - Nguyen, Steve

AU - Mann, Matthias

AU - Nielsen, Michael L

N1 - Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved.

PY - 2014/2/13

Y1 - 2014/2/13

N2 - Phosphoinositides (PIPs) play key roles in signaling and disease. Using high-resolution quantitative mass spectrometry, we identified PIP-interacting proteins and profiled their binding specificities toward all seven PIP variants. This analysis revealed 405 PIP-binding proteins, which is greater than the total number of phospho- or ubiquitin-binding domains. Translocation and inhibitor assays of identified PIP-binding proteins confirmed that our methodology targets direct interactors. The PIP interactome encompasses proteins from diverse cellular compartments, prominently including the nucleus. Our data set revealed a consensus motif for PI(3,4,5)P3-interacting pleckstrin homology (PH) domains, which enabled in silico identification of phosphoinositide interactors. Members of the dedicator of cytokinesis family C exhibited specificity toward both PI(3,4,5)P3 and PI(4,5)P2. Structurally, this dual specificity is explained by a decreased number of positively charged residues in the L1 subdomain compared with DOCK1. The presented PIP-binding proteome and its specificity toward individual PIPs should be a valuable resource for the community.

AB - Phosphoinositides (PIPs) play key roles in signaling and disease. Using high-resolution quantitative mass spectrometry, we identified PIP-interacting proteins and profiled their binding specificities toward all seven PIP variants. This analysis revealed 405 PIP-binding proteins, which is greater than the total number of phospho- or ubiquitin-binding domains. Translocation and inhibitor assays of identified PIP-binding proteins confirmed that our methodology targets direct interactors. The PIP interactome encompasses proteins from diverse cellular compartments, prominently including the nucleus. Our data set revealed a consensus motif for PI(3,4,5)P3-interacting pleckstrin homology (PH) domains, which enabled in silico identification of phosphoinositide interactors. Members of the dedicator of cytokinesis family C exhibited specificity toward both PI(3,4,5)P3 and PI(4,5)P2. Structurally, this dual specificity is explained by a decreased number of positively charged residues in the L1 subdomain compared with DOCK1. The presented PIP-binding proteome and its specificity toward individual PIPs should be a valuable resource for the community.

U2 - 10.1016/j.celrep.2013.12.038

DO - 10.1016/j.celrep.2013.12.038

M3 - Journal article

C2 - 24462288

VL - 6

SP - 578

EP - 591

JO - Cell Reports

JF - Cell Reports

SN - 2211-1247

IS - 3

ER -

ID: 101063410