A unified nomenclature and amino acid numbering for human PTEN

Rafael Pulido; Suzanne J Baker; Joao T Barata; Arkaitz Carracedo; Victor J Cid; Ian D Chin-Sang; Vrushank Davé; Jeroen den Hertog; Peter Devreotes; Britta J Eickholt; Charis Eng; Frank B Furnari; Maria-Magdalena Georgescu; Arne Gericke; Benjamin Hopkins; Xeujun Jiang; Seung-Rock Lee; Mathias Lösche; Prerna Malaney; Xavier Matias-Guiu; María Molina; Pier Paolo Pandolfi; Ramon Parsons; Paolo Pinton; Carmen Rivas; Rafael M Rocha; Manuel S Rodríguez; Alonzo H Ross; Manuel Serrano; Vuk Stambolic; Bangyan Stiles; Akira Suzuki; Seong-Seng Tan; Nicholas K Tonks; Lloyd C Trotman; Nicolas Wolff; Rudiger Woscholski; Hong Wu; Nicholas R Leslie

doi:10.1126/scisignal.2005560

A unified nomenclature and amino acid numbering for human PTEN

Rafael Pulido, Suzanne J Baker, Joao T Barata, Arkaitz Carracedo, Victor J Cid, Ian D Chin-Sang, Vrushank Davé, Jeroen den Hertog, Peter Devreotes, Britta J Eickholt, Charis Eng, Frank B Furnari, Maria-Magdalena Georgescu, Arne Gericke, Benjamin Hopkins, Xeujun Jiang, Seung-Rock Lee, Mathias Lösche, Prerna Malaney, Xavier Matias-GuiuMaría Molina, Pier Paolo Pandolfi, Ramon Parsons, Paolo Pinton, Carmen Rivas, Rafael M Rocha, Manuel S Rodríguez, Alonzo H Ross, Manuel Serrano, Vuk Stambolic, Bangyan Stiles, Akira Suzuki, Seong-Seng Tan, Nicholas K Tonks, Lloyd C Trotman, Nicolas Wolff, Rudiger Woscholski, Hong Wu, Nicholas R Leslie

Hubrecht Institute

Onderzoeksoutput: Bijdrage aan wetenschappelijk tijdschrift/periodieke uitgave › Artikel › Wetenschappelijk › peer review

51 Citaten (Scopus)

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The tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.

Originele taal-2	Engels
Pagina's (van-tot)	pe15
Tijdschrift	Science Signaling
Volume	7
Nummer van het tijdschrift	332
DOI's	https://doi.org/10.1126/scisignal.2005560
Status	Gepubliceerd - 01 jul. 2014

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Pulido, R., Baker, S. J., Barata, J. T., Carracedo, A., Cid, V. J., Chin-Sang, I. D., Davé, V., den Hertog, J., Devreotes, P., Eickholt, B. J., Eng, C., Furnari, F. B., Georgescu, M.-M., Gericke, A., Hopkins, B., Jiang, X., Lee, S.-R., Lösche, M., Malaney, P., ... Leslie, N. R. (2014). A unified nomenclature and amino acid numbering for human PTEN. Science Signaling, 7(332), pe15. https://doi.org/10.1126/scisignal.2005560

@article{23546177f27e41ef9329cb6721e92b4b,

title = "A unified nomenclature and amino acid numbering for human PTEN",

abstract = "The tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.",

author = "Rafael Pulido and Baker, {Suzanne J} and Barata, {Joao T} and Arkaitz Carracedo and Cid, {Victor J} and Chin-Sang, {Ian D} and Vrushank Dav{\'e} and {den Hertog}, Jeroen and Peter Devreotes and Eickholt, {Britta J} and Charis Eng and Furnari, {Frank B} and Maria-Magdalena Georgescu and Arne Gericke and Benjamin Hopkins and Xeujun Jiang and Seung-Rock Lee and Mathias L{\"o}sche and Prerna Malaney and Xavier Matias-Guiu and Mar{\'i}a Molina and Pandolfi, {Pier Paolo} and Ramon Parsons and Paolo Pinton and Carmen Rivas and Rocha, {Rafael M} and Rodr{\'i}guez, {Manuel S} and Ross, {Alonzo H} and Manuel Serrano and Vuk Stambolic and Bangyan Stiles and Akira Suzuki and Seong-Seng Tan and Tonks, {Nicholas K} and Trotman, {Lloyd C} and Nicolas Wolff and Rudiger Woscholski and Hong Wu and Leslie, {Nicholas R}",

note = "Copyright {\textcopyright} 2014, American Association for the Advancement of Science.",

year = "2014",

month = jul,

day = "1",

doi = "10.1126/scisignal.2005560",

language = "English",

volume = "7",

pages = "pe15",

journal = "Science Signaling",

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publisher = "American Association for the Advancement of Science (AAAS)",

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Pulido, R, Baker, SJ, Barata, JT, Carracedo, A, Cid, VJ, Chin-Sang, ID, Davé, V, den Hertog, J, Devreotes, P, Eickholt, BJ, Eng, C, Furnari, FB, Georgescu, M-M, Gericke, A, Hopkins, B, Jiang, X, Lee, S-R, Lösche, M, Malaney, P, Matias-Guiu, X, Molina, M, Pandolfi, PP, Parsons, R, Pinton, P, Rivas, C, Rocha, RM, Rodríguez, MS, Ross, AH, Serrano, M, Stambolic, V, Stiles, B, Suzuki, A, Tan, S-S, Tonks, NK, Trotman, LC, Wolff, N, Woscholski, R, Wu, H & Leslie, NR 2014, 'A unified nomenclature and amino acid numbering for human PTEN', Science Signaling, vol. 7, nr. 332, blz. pe15. https://doi.org/10.1126/scisignal.2005560

TY - JOUR

T1 - A unified nomenclature and amino acid numbering for human PTEN

AU - Pulido, Rafael

AU - Baker, Suzanne J

AU - Barata, Joao T

AU - Carracedo, Arkaitz

AU - Cid, Victor J

AU - Chin-Sang, Ian D

AU - Davé, Vrushank

AU - den Hertog, Jeroen

AU - Devreotes, Peter

AU - Eickholt, Britta J

AU - Eng, Charis

AU - Furnari, Frank B

AU - Georgescu, Maria-Magdalena

AU - Gericke, Arne

AU - Hopkins, Benjamin

AU - Jiang, Xeujun

AU - Lee, Seung-Rock

AU - Lösche, Mathias

AU - Malaney, Prerna

AU - Matias-Guiu, Xavier

AU - Molina, María

AU - Pandolfi, Pier Paolo

AU - Parsons, Ramon

AU - Pinton, Paolo

AU - Rivas, Carmen

AU - Rocha, Rafael M

AU - Rodríguez, Manuel S

AU - Ross, Alonzo H

AU - Serrano, Manuel

AU - Stambolic, Vuk

AU - Stiles, Bangyan

AU - Suzuki, Akira

AU - Tan, Seong-Seng

AU - Tonks, Nicholas K

AU - Trotman, Lloyd C

AU - Wolff, Nicolas

AU - Woscholski, Rudiger

AU - Wu, Hong

AU - Leslie, Nicholas R

PY - 2014/7/1

Y1 - 2014/7/1

N2 - The tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.

AB - The tumor suppressor PTEN is a major brake for cell transformation, mainly due to its phosphatidylinositol 3,4,5-trisphosphate [PI(3,4,5)P3] phosphatase activity that directly counteracts the oncogenicity of phosphoinositide 3-kinase (PI3K). PTEN mutations are frequent in tumors and in the germ line of patients with tumor predisposition or with neurological or cognitive disorders, which makes the PTEN gene and protein a major focus of interest in current biomedical research. After almost two decades of intense investigation on the 403-residue-long PTEN protein, a previously uncharacterized form of PTEN has been discovered that contains 173 amino-terminal extra amino acids, as a result of an alternate translation initiation site. To facilitate research in the field and to avoid ambiguities in the naming and identification of PTEN amino acids from publications and databases, we propose here a unifying nomenclature and amino acid numbering for this longer form of PTEN.

U2 - 10.1126/scisignal.2005560

DO - 10.1126/scisignal.2005560

M3 - Article

C2 - 24985344

SN - 1937-9145

VL - 7

SP - pe15

JO - Science Signaling

JF - Science Signaling

IS - 332

ER -

A unified nomenclature and amino acid numbering for human PTEN

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