Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Fine-Tuning Limited Proteolysis : A Major Role for Regulated Site-Specific O-Glycosylation. / Goth, Christoffer K.; Vakhrushev, Sergey Y.; Joshi, Hiren J.; Clausen, Henrik; Schjoldager, Katrine T.

I: Trends in Biochemical Sciences, Bind 43, Nr. 4, 2018, s. 269-284.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Goth, CK, Vakhrushev, SY, Joshi, HJ, Clausen, H & Schjoldager, KT 2018, 'Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation', Trends in Biochemical Sciences, bind 43, nr. 4, s. 269-284. https://doi.org/10.1016/j.tibs.2018.02.005

APA

Goth, C. K., Vakhrushev, S. Y., Joshi, H. J., Clausen, H., & Schjoldager, K. T. (2018). Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation. Trends in Biochemical Sciences, 43(4), 269-284. https://doi.org/10.1016/j.tibs.2018.02.005

Vancouver

Goth CK, Vakhrushev SY, Joshi HJ, Clausen H, Schjoldager KT. Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation. Trends in Biochemical Sciences. 2018;43(4):269-284. https://doi.org/10.1016/j.tibs.2018.02.005

Author

Goth, Christoffer K. ; Vakhrushev, Sergey Y. ; Joshi, Hiren J. ; Clausen, Henrik ; Schjoldager, Katrine T. / Fine-Tuning Limited Proteolysis : A Major Role for Regulated Site-Specific O-Glycosylation. I: Trends in Biochemical Sciences. 2018 ; Bind 43, Nr. 4. s. 269-284.

Bibtex

@article{ca906aa6c9b3418698dfdd12b8b973b3,
title = "Fine-Tuning Limited Proteolysis: A Major Role for Regulated Site-Specific O-Glycosylation",
abstract = "Limited proteolytic processing is an essential and ubiquitous post-translational modification (PTM) affecting secreted proteins; failure to regulate the process is often associated with disease. Glycosylation is also a ubiquitous protein PTM and site-specific O-glycosylation in close proximity to sites of proteolysis can regulate and direct the activity of proprotein convertases, a disintegrin and metalloproteinases (ADAMs), and metalloproteinases affecting the activation or inactivation of many classes of proteins, including G-protein-coupled receptors (GPCRs). Here, we summarize the emerging data that suggest O-glycosylation to be a key regulator of limited proteolysis, and highlight the potential for crosstalk between multiple PTMs.",
keywords = "G-protein-coupled receptors, GalNAc-Ts, O-glycosylation, proteases, proteolytic processing, PTM",
author = "Goth, {Christoffer K.} and Vakhrushev, {Sergey Y.} and Joshi, {Hiren J.} and Henrik Clausen and Schjoldager, {Katrine T.}",
year = "2018",
doi = "10.1016/j.tibs.2018.02.005",
language = "English",
volume = "43",
pages = "269--284",
journal = "Trends in Biochemical Sciences",
issn = "0968-0004",
publisher = "Elsevier",
number = "4",

}

RIS

TY - JOUR

T1 - Fine-Tuning Limited Proteolysis

T2 - A Major Role for Regulated Site-Specific O-Glycosylation

AU - Goth, Christoffer K.

AU - Vakhrushev, Sergey Y.

AU - Joshi, Hiren J.

AU - Clausen, Henrik

AU - Schjoldager, Katrine T.

PY - 2018

Y1 - 2018

N2 - Limited proteolytic processing is an essential and ubiquitous post-translational modification (PTM) affecting secreted proteins; failure to regulate the process is often associated with disease. Glycosylation is also a ubiquitous protein PTM and site-specific O-glycosylation in close proximity to sites of proteolysis can regulate and direct the activity of proprotein convertases, a disintegrin and metalloproteinases (ADAMs), and metalloproteinases affecting the activation or inactivation of many classes of proteins, including G-protein-coupled receptors (GPCRs). Here, we summarize the emerging data that suggest O-glycosylation to be a key regulator of limited proteolysis, and highlight the potential for crosstalk between multiple PTMs.

AB - Limited proteolytic processing is an essential and ubiquitous post-translational modification (PTM) affecting secreted proteins; failure to regulate the process is often associated with disease. Glycosylation is also a ubiquitous protein PTM and site-specific O-glycosylation in close proximity to sites of proteolysis can regulate and direct the activity of proprotein convertases, a disintegrin and metalloproteinases (ADAMs), and metalloproteinases affecting the activation or inactivation of many classes of proteins, including G-protein-coupled receptors (GPCRs). Here, we summarize the emerging data that suggest O-glycosylation to be a key regulator of limited proteolysis, and highlight the potential for crosstalk between multiple PTMs.

KW - G-protein-coupled receptors

KW - GalNAc-Ts

KW - O-glycosylation

KW - proteases

KW - proteolytic processing

KW - PTM

U2 - 10.1016/j.tibs.2018.02.005

DO - 10.1016/j.tibs.2018.02.005

M3 - Review

C2 - 29506880

AN - SCOPUS:85042631647

VL - 43

SP - 269

EP - 284

JO - Trends in Biochemical Sciences

JF - Trends in Biochemical Sciences

SN - 0968-0004

IS - 4

ER -

ID: 195255835