(Q24290417)

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The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation

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The tumor suppressor PTEN is phosphorylated by the protein kinase CK2 at its C terminus. Implications for PTEN stability to proteasome-mediated degradation (English)

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phosphorylation

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Casein kinase 2 alpha 1

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GOA release 2020-03-11

protein serine/threonine kinase activity

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GOA release 2020-03-11

author name string

J Torres

1

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R Pulido

2

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language of work or name

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publication date

12 January 2001

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Journal of Biological Chemistry

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276

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993-8

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2

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The ubiquitin-proteasome proteolytic pathway

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Casein kinase 2: an 'eminence grise' in cellular regulation?

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The multiple roles of PTEN in tumor suppression

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Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association

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Heterogeneous lack of expression of the tumour suppressor PTEN protein in human neoplastic tissues

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Proteasome inhibitors: valuable new tools for cell biologists

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PTEN: a tumour suppressor that functions as a phospholipid phosphatase

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Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers

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Analysis of the cellular functions of PTEN using catalytic domain and C-terminal mutations: differential effects of C-terminal deletion on signalling pathways downstream of phosphoinositide 3-kinase

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Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2

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Inducible expression of protein kinase CK2 in mammalian cells. Evidence for functional specialization of CK2 isoforms.

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Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase

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Signaling through scaffold, anchoring, and adaptor proteins

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Identifiers

10.1074/JBC.M009134200

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

1 reference

Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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