Cited by 391Protein Tyrosine PhosphatasesProtein Kinase Regulation and GTPase SignalingSignaling Pathways in Disease

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PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail)

Janssens, Veerle, Longin, Sari, Goris, Jozef·2008·Trends in Biochemical Sciences

DOI 10.1016/j.tibs.2007.12.004

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Abstract

Protein phosphatase 2A (PP2A), a major phospho-serine/threonine phosphatase, is conserved throughout eukaryotes. It dephosphorylates a plethora of cellular proteins, including kinases and other signaling molecules involved in cell division, gene regulation, protein synthesis and cytoskeleton organization. PP2A enzymes typically exist as heterotrimers comprising catalytic C-, structural A- and regulatory B-type subunits. The B-type subunits function as targeting and substrate-specificity factors; hence, holoenzyme assembly with the appropriate B-type subunit is crucial for PP2A specificity and regulation. Recently, several biochemical and structural determinants have been described that affect PP2A holoenzyme assembly. Moreover, the effects of specific post-translational modifications of the C-terminal tail of the catalytic subunit indicate that a 'code' might regulate dynamic exchange of regulatory B-type subunits, thus affecting the specificity of PP2A.

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Authors: Janssens, V., Longin, S., & Goris, J.
Affiliations: KU Leuven (BE)
Corresponding author: Goris, Jozef
ORCID: Janssens, Veerle
Venue: Trends in Biochemical Sciences
Publisher: Elsevier BV
Published: 2008-03
Volume: 33
Issue: 3
Pages: 113-121
ISSN: 0968-0004 (ISSN-L)
DOI: 10.1016/j.tibs.2007.12.004
OpenAlex: W2165421630
Cited by: 390
References: 77
Citations by year: 2026: 2 · 2025: 9 · 2024: 8 · 2023: 18 · 2022: 19 · 2021: 16 · 2020: 17 · 2019: 21 · 2018: 15 · 2017: 25 · 2016: 29 · 2015: 17 · 2014: 33 · 2013: 37 · 2012: 31
FWCI: 2.39
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Trends in Biochemical Sciences (publishedVersion)
PubMed (publishedVersion)
Lirias (submittedVersion)
Funders: Fonds Wetenschappelijk Onderzoek
Vlaamse regering
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: protein phosphatase 2A, post-translational modification, substrate specificity, phosphatase regulation, Caenorhabditis elegans
MeSH terms: Animals, Catalysis, Humans, Models, Biological, Protein Conformation, Substrate Specificity, Protein Structure, Secondary, Holoenzymes, Protein Subunits, Protein Phosphatase 2

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PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail)

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