Towards dissecting the mechanism of protein phosphatase‐1 inhibition by its c‐terminal phosphorylation

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Abstract: Phosphoprotein phosphatase‐1 (PP1) is a key player in the regulation of phospho‐serine (pSer) and phospho‐threonine (pThr) dephosphorylation and is involved in a large fraction of cellular signaling pathways. Aberrant activity of PP1 has been linked to many diseases, including cancer and heart failure. Besides a well‐established activity control by regulatory proteins, an inhibitory function for phosphorylation (p) of a Thr residue in the C‐terminal intrinsically disordered tail of PP1 has been demonstrated. The associated phenotype of cell‐cycle arrest was repeatedly proposed to be due to autoinhibition of PP1 through either conformational changes or substrate competition. Here, we use PP1 variants created by mutations and protein semisynthesis to differentiate between these hypotheses. Our data support the hypothesis that pThr exerts its inhibitory function by mediating protein complex formation rather than by a direct mechanism of structural changes or substrate competition

Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Notes: ChemBioChem. - 22, 5 (2021) , 834-838, ISSN: 1439-7633

Event: Veröffentlichung

(where): Freiburg

(who): Universität

(when): 2021

Creator: Salvi, Francesca
Hoermann, Bernhard
Pino García, Javier
Fontanillo, Miriam
Derua, Rita
Beullens, Monique
Bollen, Mathieu
Barabas, Orsolya
Köhn, Maja

DOI: 10.1002/cbic.202000669

URN: urn:nbn:de:bsz:25-freidok-1941581

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 25.03.2025, 1:46 PM CET

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Associated

Salvi, Francesca
Hoermann, Bernhard
Pino García, Javier
Fontanillo, Miriam
Derua, Rita
Beullens, Monique
Bollen, Mathieu
Barabas, Orsolya
Köhn, Maja
Universität

Time of origin

2021

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Towards dissecting the mechanism of protein phosphatase‐1 inhibition by its c‐terminal phosphorylation

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Other Objects (12)

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