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Identification of the human testis protein phosphatase 1 interactome

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Identification of the human testis protein phosphatase 1 interactome. / Fardilha, Margarida (Lead / Corresponding author); Esteves, Sara L. C.; Korrodi-Gregório, Luis; Vintém, Ana Paula; Domingues, Sara C.; Rebelo, Sandra; Morrice, Nick; Cohen, Patricia T. W.; da cruz e silva, Odette A. B.; da cruz e silva, Edgar F.

In: Biochemical Pharmacology, Vol. 82, No. 10, 2011, p. 1403-1415.

Research output: Contribution to journalArticle

Harvard

Fardilha, M, Esteves, SLC, Korrodi-Gregório, L, Vintém, AP, Domingues, SC, Rebelo, S, Morrice, N, Cohen, PTW, da cruz e silva, OAB & da cruz e silva, EF 2011, 'Identification of the human testis protein phosphatase 1 interactome' Biochemical Pharmacology, vol 82, no. 10, pp. 1403-1415., 10.1016/j.bcp.2011.02.018

APA

Fardilha, M., Esteves, S. L. C., Korrodi-Gregório, L., Vintém, A. P., Domingues, S. C., Rebelo, S., ... da cruz e silva, E. F. (2011). Identification of the human testis protein phosphatase 1 interactome. Biochemical Pharmacology, 82(10), 1403-1415. 10.1016/j.bcp.2011.02.018

Vancouver

Fardilha M, Esteves SLC, Korrodi-Gregório L, Vintém AP, Domingues SC, Rebelo S et al. Identification of the human testis protein phosphatase 1 interactome. Biochemical Pharmacology. 2011;82(10):1403-1415. Available from: 10.1016/j.bcp.2011.02.018

Author

Fardilha, Margarida (Lead / Corresponding author); Esteves, Sara L. C.; Korrodi-Gregório, Luis; Vintém, Ana Paula; Domingues, Sara C.; Rebelo, Sandra; Morrice, Nick; Cohen, Patricia T. W.; da cruz e silva, Odette A. B.; da cruz e silva, Edgar F. / Identification of the human testis protein phosphatase 1 interactome.

In: Biochemical Pharmacology, Vol. 82, No. 10, 2011, p. 1403-1415.

Research output: Contribution to journalArticle

Bibtex - Download

@article{8a71c75953da40cf9453544ded0890ce,
title = "Identification of the human testis protein phosphatase 1 interactome",
author = "Margarida Fardilha and Esteves, {Sara L. C.} and Luis Korrodi-Gregório and Vintém, {Ana Paula} and Domingues, {Sara C.} and Sandra Rebelo and Nick Morrice and Cohen, {Patricia T. W.} and {da cruz e silva}, {Odette A. B.} and {da cruz e silva}, {Edgar F.}",
year = "2011",
doi = "10.1016/j.bcp.2011.02.018",
volume = "82",
number = "10",
pages = "1403--1415",
journal = "Biochemical Pharmacology",
issn = "0006-2952",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Identification of the human testis protein phosphatase 1 interactome

A1 - Fardilha,Margarida

A1 - Esteves,Sara L. C.

A1 - Korrodi-Gregório,Luis

A1 - Vintém,Ana Paula

A1 - Domingues,Sara C.

A1 - Rebelo,Sandra

A1 - Morrice,Nick

A1 - Cohen,Patricia T. W.

A1 - da cruz e silva,Odette A. B.

A1 - da cruz e silva,Edgar F.

AU - Fardilha,Margarida

AU - Esteves,Sara L. C.

AU - Korrodi-Gregório,Luis

AU - Vintém,Ana Paula

AU - Domingues,Sara C.

AU - Rebelo,Sandra

AU - Morrice,Nick

AU - Cohen,Patricia T. W.

AU - da cruz e silva,Odette A. B.

AU - da cruz e silva,Edgar F.

PY - 2011

Y1 - 2011

N2 - Protein phosphorylation is a critical regulatory mechanism in cellular signalling. To this end, PP1 is a major eukaryotic serine/threonine-specific phosphatase whose cellular functions, in turn, depend on complexes it forms with PP1 interacting proteins - PIPs. The importance of the testis/sperm-enriched variant, PP1?2, in sperm motility and spermatogenesis has previously been shown. Given the key role of PIPs, it is imperative to identify the physiologically relevant PIPs in testis and sperm. Hence, we performed Yeast Two-Hybrid screens of a human testis cDNA library using as baits the different PP1 isoforms and also a proteomic approach aimed at identifying PP1?2 binding proteins. To the best of our knowledge this is the largest data set of the human testis PP1 interactome. We report the identification of 77 proteins in human testis and 7 proteins in human sperm that bind PP1. The data obtained increased the known PP1 interactome by reporting 72 novel interactions. Confirmation of the interaction of PP1 with 5 different proteins was also further validated by co-immunoprecipitation or protein overlays. The data here presented provides important insights towards the function of these proteins and opens new possibilities for future research. In fact, such diversity in PP1 regulators makes them excellent targets for pharmacological intervention. © 2011 Elsevier Inc. All rights reserved.

AB - Protein phosphorylation is a critical regulatory mechanism in cellular signalling. To this end, PP1 is a major eukaryotic serine/threonine-specific phosphatase whose cellular functions, in turn, depend on complexes it forms with PP1 interacting proteins - PIPs. The importance of the testis/sperm-enriched variant, PP1?2, in sperm motility and spermatogenesis has previously been shown. Given the key role of PIPs, it is imperative to identify the physiologically relevant PIPs in testis and sperm. Hence, we performed Yeast Two-Hybrid screens of a human testis cDNA library using as baits the different PP1 isoforms and also a proteomic approach aimed at identifying PP1?2 binding proteins. To the best of our knowledge this is the largest data set of the human testis PP1 interactome. We report the identification of 77 proteins in human testis and 7 proteins in human sperm that bind PP1. The data obtained increased the known PP1 interactome by reporting 72 novel interactions. Confirmation of the interaction of PP1 with 5 different proteins was also further validated by co-immunoprecipitation or protein overlays. The data here presented provides important insights towards the function of these proteins and opens new possibilities for future research. In fact, such diversity in PP1 regulators makes them excellent targets for pharmacological intervention. © 2011 Elsevier Inc. All rights reserved.

UR - http://www.scopus.com/inward/record.url?scp=80054708627&partnerID=8YFLogxK

U2 - 10.1016/j.bcp.2011.02.018

DO - 10.1016/j.bcp.2011.02.018

M1 - Article

JO - Biochemical Pharmacology

JF - Biochemical Pharmacology

SN - 0006-2952

IS - 10

VL - 82

SP - 1403

EP - 1415

ER -

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