Functions of intrinsic disorder in transmembrane proteins

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Standard

Functions of intrinsic disorder in transmembrane proteins. / Kjaergaard, Magnus; Kragelund, Birthe B.

I: Cellular and Molecular Life Sciences, Bind 74, Nr. 17, 01.09.2017, s. 3205-3224.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisReviewForskningpeer review

Harvard

Kjaergaard, M & Kragelund, BB 2017, 'Functions of intrinsic disorder in transmembrane proteins', Cellular and Molecular Life Sciences, bind 74, nr. 17, s. 3205-3224. https://doi.org/10.1007/s00018-017-2562-5

APA

Kjaergaard, M., & Kragelund, B. B. (2017). Functions of intrinsic disorder in transmembrane proteins. Cellular and Molecular Life Sciences, 74(17), 3205-3224. https://doi.org/10.1007/s00018-017-2562-5

CBE

Kjaergaard M, Kragelund BB. 2017. Functions of intrinsic disorder in transmembrane proteins. Cellular and Molecular Life Sciences. 74(17):3205-3224. https://doi.org/10.1007/s00018-017-2562-5

MLA

Kjaergaard, Magnus og Birthe B. Kragelund. "Functions of intrinsic disorder in transmembrane proteins". Cellular and Molecular Life Sciences. 2017, 74(17). 3205-3224. https://doi.org/10.1007/s00018-017-2562-5

Vancouver

Kjaergaard M, Kragelund BB. Functions of intrinsic disorder in transmembrane proteins. Cellular and Molecular Life Sciences. 2017 sep 1;74(17):3205-3224. https://doi.org/10.1007/s00018-017-2562-5

Author

Kjaergaard, Magnus ; Kragelund, Birthe B. / Functions of intrinsic disorder in transmembrane proteins. I: Cellular and Molecular Life Sciences. 2017 ; Bind 74, Nr. 17. s. 3205-3224.

Bibtex

@article{6c9096ba454248f2be6e6382b1debf4e,
title = "Functions of intrinsic disorder in transmembrane proteins",
abstract = "Intrinsic disorder is common in integral membrane proteins, particularly in the intracellular domains. Despite this observation, these domains are not always recognized as being disordered. In this review, we will discuss the biological functions of intrinsically disordered regions of membrane proteins, and address why the flexibility afforded by disorder is mechanistically important. Intrinsically disordered regions are present in many common classes of membrane proteins including ion channels and transporters; G-protein coupled receptors (GPCRs), receptor tyrosine kinases and cytokine receptors. The functions of the disordered regions are many and varied. We will discuss selected examples including: (1) Organization of receptors, kinases, phosphatases and second messenger sources into signaling complexes. (2) Modulation of the membrane-embedded domain function by ball-and-chain like mechanisms. (3) Trafficking of membrane proteins. (4) Transient membrane associations. (5) Post-translational modifications most notably phosphorylation and (6) disorder-linked isoform dependent function. We finish the review by discussing the future challenges facing the membrane protein community regarding protein disorder.",
keywords = "Ball-and-chain inhibition, Intrinsically disordered protein, Lipid interaction domain, Membrane protein, Receptor associated signalling complex",
author = "Magnus Kjaergaard and Kragelund, {Birthe B.}",
year = "2017",
month = "9",
day = "1",
doi = "10.1007/s00018-017-2562-5",
language = "English",
volume = "74",
pages = "3205--3224",
journal = "Cellular and Molecular Life Sciences",
issn = "1420-682X",
publisher = "Springer Basel AG",
number = "17",

}

RIS

TY - JOUR

T1 - Functions of intrinsic disorder in transmembrane proteins

AU - Kjaergaard, Magnus

AU - Kragelund, Birthe B.

PY - 2017/9/1

Y1 - 2017/9/1

N2 - Intrinsic disorder is common in integral membrane proteins, particularly in the intracellular domains. Despite this observation, these domains are not always recognized as being disordered. In this review, we will discuss the biological functions of intrinsically disordered regions of membrane proteins, and address why the flexibility afforded by disorder is mechanistically important. Intrinsically disordered regions are present in many common classes of membrane proteins including ion channels and transporters; G-protein coupled receptors (GPCRs), receptor tyrosine kinases and cytokine receptors. The functions of the disordered regions are many and varied. We will discuss selected examples including: (1) Organization of receptors, kinases, phosphatases and second messenger sources into signaling complexes. (2) Modulation of the membrane-embedded domain function by ball-and-chain like mechanisms. (3) Trafficking of membrane proteins. (4) Transient membrane associations. (5) Post-translational modifications most notably phosphorylation and (6) disorder-linked isoform dependent function. We finish the review by discussing the future challenges facing the membrane protein community regarding protein disorder.

AB - Intrinsic disorder is common in integral membrane proteins, particularly in the intracellular domains. Despite this observation, these domains are not always recognized as being disordered. In this review, we will discuss the biological functions of intrinsically disordered regions of membrane proteins, and address why the flexibility afforded by disorder is mechanistically important. Intrinsically disordered regions are present in many common classes of membrane proteins including ion channels and transporters; G-protein coupled receptors (GPCRs), receptor tyrosine kinases and cytokine receptors. The functions of the disordered regions are many and varied. We will discuss selected examples including: (1) Organization of receptors, kinases, phosphatases and second messenger sources into signaling complexes. (2) Modulation of the membrane-embedded domain function by ball-and-chain like mechanisms. (3) Trafficking of membrane proteins. (4) Transient membrane associations. (5) Post-translational modifications most notably phosphorylation and (6) disorder-linked isoform dependent function. We finish the review by discussing the future challenges facing the membrane protein community regarding protein disorder.

KW - Ball-and-chain inhibition

KW - Intrinsically disordered protein

KW - Lipid interaction domain

KW - Membrane protein

KW - Receptor associated signalling complex

UR - http://www.scopus.com/inward/record.url?scp=85020640871&partnerID=8YFLogxK

U2 - 10.1007/s00018-017-2562-5

DO - 10.1007/s00018-017-2562-5

M3 - Review

VL - 74

SP - 3205

EP - 3224

JO - Cellular and Molecular Life Sciences

JF - Cellular and Molecular Life Sciences

SN - 1420-682X

IS - 17

ER -