The DOI matches its Crossref record; 76 of the 77 references it cites were found in a registry or an index.
PP2A holoenzyme assembly: in cauda venenum (the sting is in the tail)
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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In the citing paper
“The unstructured C-terminus of PP2A/C is subject to post-translational modifications during the process of trimeric PP2A biogenesis, including phosphorylation of T304 and Y307 and carboxymethylation on L309 (Janssens et al., 2008; Lee and Pallas, 2007; Löw et al., 2014).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Janssens et al., 2008
In the citing paper
“Besides twenty PP2A subunit encoding genes, some of which are tissue-specifically expressed, five additional genes encode major regulators of active PP2A trimer assembly, and at least seven genes encode cellular PP2A inhibitors”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [13]
In the citing paper
“the PME-1 and LCMT-1 transgenic models provide nevertheless further evidence for a role of these PP2A trimers in tau dephosphorylation, and additionally, in the regulation of APP phosphorylation.”
From Physiologic functions of PP2A: Lessons from genetically modified mice (2019) · cites this paper as [13]
In the citing paper
“Initial studies have pointed to the reversible methylation of a specific residue (L309) at the C-terminal tail of the catalytic subunit [ 63 – 65 ]. This modification appears to be critical in modulating the binding affinity of the regulatory subunit, contributing to the formation of distinct heterotrimeric complexes.”
From Targeting PP2A in cancer: an underrated option (2025) · cites this paper as [64]
Citations
Cites
1 retracted
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RetractedJanssens, V., & Goris, J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530417 · Cited by 1,927
Self-citationYeh, E., Cunningham, M., Arnold, H., Chasse, D., Monteith, T., Ivaldi, G., Hahn, W. C., Stukenberg, P. T., Shenolikar, S., Uchida, T., et al. (2004) · Nature Cell Biology · doi:10.1038/ncb1110 · Cited by 791
CIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677
Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation
Chen, J., Martin, B. L., & Brautigan, D. L. (1992) · Science · doi:10.1126/science.1325671 · Cited by 601
Neviani, P., Santhanam, R., Trotta, R., Notari, M., Blaser, B. W., Liu, S., Mao, H. C., Chang, J. S., Galietta, A., Uttam, A., et al. (2005) · Cancer Cell · doi:10.1016/j.ccr.2005.10.015 · Cited by 481
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Cho, U. S., & Xu, W. (2007) · Nature · doi:10.1038/nature05351 · Cited by 459
Structure of the Protein Phosphatase 2A Holoenzyme
Xu, Y., Xing, Y., Chen, Y., Chao, Y., Lin, Z., Fan, E., Yu, J. W., Strack, S., Jeffrey, P. D., & Shi, Y. (2006) · Cell · doi:10.1016/j.cell.2006.11.033 · Cited by 450
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PP2A: the expected tumor suppressor
Janssens, V., Goris, J., & Van Hoof, C. (2005) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2004.12.004 · Cited by 426
Self-citation
Research works printed but not linked: 1
- Kamibayashi, 1995, Control of protein phosphatase 2A by multiple families of regulatory subunits, Adv. Protein Phosphatases, 9, 195
Cited by
Sorted by citations
Serine/threonine phosphatases: mechanism through structure
Shi, Y. (2009) · Cell · doi:10.1016/j.cell.2009.10.006 · Cited by 1,488
Wnt/β-catenin signaling in cancers and targeted therapies
Yu, F., Yu, C., Li, F., Zuo, Y., Wang, Y., Yao, L., Wu, C., Wang, C., & Ye, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00701-5 · Cited by 734
From Promiscuity to Precision: Protein Phosphatases Get a Makeover
Virshup, D. M., & Shenolikar, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.02.015 · Cited by 643
Clouse, S. D. (2011) · The Plant Cell · doi:10.1105/tpc.111.084475 · Cited by 573
The extended PP1 toolkit: designed to create specificity
Bollen, M., Peti, W., Ragusa, M. J., & Beullens, M. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.03.002 · Cited by 524
Metadata
- 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)
- 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
- 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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