TY - JOUR
T1 - Decoding the PTM-switchboard of Notch
AU - Antfolk, Daniel
AU - Antila, Christian
AU - Kemppainen, Kati
AU - Landor, Sebastian K.J.
AU - Sahlgren, Cecilia
PY - 2019/12/1
Y1 - 2019/12/1
N2 - The developmentally indispensable Notch pathway exhibits a high grade of pleiotropism in its biological output. Emerging evidence supports the notion of post-translational modifications (PTMs) as a modus operandi controlling dynamic fine-tuning of Notch activity. Although, the intricacy of Notch post-translational regulation, as well as how these modifications lead to multiples of divergent Notch phenotypes is still largely unknown, numerous studies show a correlation between the site of modification and the output. These include glycosylation of the extracellular domain of Notch modulating ligand binding, and phosphorylation of the PEST domain controlling half-life of the intracellular domain of Notch. Furthermore, several reports show that multiple PTMs can act in concert, or compete for the same sites to drive opposite outputs. However, further investigation of the complex PTM crosstalk is required for a complete understanding of the PTM-mediated Notch switchboard. In this review, we aim to provide a consistent and up-to-date summary of the currently known PTMs acting on the Notch signaling pathway, their functions in different contexts, as well as explore their implications in physiology and disease. Furthermore, we give an overview of the present state of PTM research methodology, and allude to a future with PTM-targeted Notch therapeutics.
AB - The developmentally indispensable Notch pathway exhibits a high grade of pleiotropism in its biological output. Emerging evidence supports the notion of post-translational modifications (PTMs) as a modus operandi controlling dynamic fine-tuning of Notch activity. Although, the intricacy of Notch post-translational regulation, as well as how these modifications lead to multiples of divergent Notch phenotypes is still largely unknown, numerous studies show a correlation between the site of modification and the output. These include glycosylation of the extracellular domain of Notch modulating ligand binding, and phosphorylation of the PEST domain controlling half-life of the intracellular domain of Notch. Furthermore, several reports show that multiple PTMs can act in concert, or compete for the same sites to drive opposite outputs. However, further investigation of the complex PTM crosstalk is required for a complete understanding of the PTM-mediated Notch switchboard. In this review, we aim to provide a consistent and up-to-date summary of the currently known PTMs acting on the Notch signaling pathway, their functions in different contexts, as well as explore their implications in physiology and disease. Furthermore, we give an overview of the present state of PTM research methodology, and allude to a future with PTM-targeted Notch therapeutics.
KW - Glycosylation
KW - Notch
KW - Phosphorylation
KW - Post-translational modifications
KW - PTM
UR - http://www.scopus.com/inward/record.url?scp=85074551997&partnerID=8YFLogxK
U2 - 10.1016/j.bbamcr.2019.07.002
DO - 10.1016/j.bbamcr.2019.07.002
M3 - Review article
C2 - 31301363
AN - SCOPUS:85074551997
VL - 1866
JO - Biochimica et Biophysica Acta, Molecular Cell Research
JF - Biochimica et Biophysica Acta, Molecular Cell Research
SN - 0167-4889
IS - 12
M1 - 118507
ER -