Screen and identification of proteins interacting with ADAM19 cytoplasmic tail

Helen Davies; Graham R. Bignell; Charles Cox; Philip Stephens; Sarah Edkins; Sheila Clegg; Jon Teague; Hayley Woffendin; Mathew J. Garnett; William Bottomley; Neil Davis; Ed Dicks; Rebecca Ewing; Yvonne Floyd; Kristian Gray; Sarah Hall; Rachel Hawes; Jaime Hughes; Vivian Kosmidou; Andrew Menzies; Catherine Mould; Adrian Parker; Claire Stevens; Stephen Watt; Steven Hooper; Hiran Jayatilake; Barry A. Gusterson; Colin Cooper; Janet Shipley; Darren Hargrave; Katherine Pritchard-Jones; Norman Maitland; Georgia Chenevix-Trench; Gregory J. Riggins; Darell D. Bigner; Giuseppe Palmieri; Antonio Cossu; Adrienne Flanagan; Andrew Nicholson; Judy W.C. Ho; Suet Y. Leung; Siu T. Yuen; Barbara L. Weber; Hilliard F. Seigler; Timothy L. Darrow; Hugh Paterson; Richard Wooster; Michael R. Stratton; P. Andrew Futreal

doi:10.1023/A:1020409217215

Screen and identification of proteins interacting with ADAM19 cytoplasmic tail

Helen Davies, Graham R. Bignell, Charles Cox, Philip Stephens, Sarah Edkins, Sheila Clegg, Jon Teague, Hayley Woffendin, Mathew J. Garnett, William Bottomley, Neil Davis, Ed Dicks, Rebecca Ewing, Yvonne Floyd, Kristian Gray, Sarah Hall, Rachel Hawes, Jaime Hughes, Vivian Kosmidou, Andrew MenziesCatherine Mould, Adrian Parker, Claire Stevens, Stephen Watt, Steven Hooper, Hiran Jayatilake, Barry A. Gusterson, Colin Cooper, Janet Shipley, Darren Hargrave, Katherine Pritchard-Jones, Norman Maitland, Georgia Chenevix-Trench, Gregory J. Riggins, Darell D. Bigner, Giuseppe Palmieri, Antonio Cossu, Adrienne Flanagan, Andrew Nicholson, Judy W.C. Ho, Suet Y. Leung, Siu T. Yuen, Barbara L. Weber, Hilliard F. Seigler, Timothy L. Darrow, Hugh Paterson, Richard Wooster, Michael R. Stratton, P. Andrew Futreal

Research output: Contribution to journal › Article › peer-review

13 Scopus citations

Abstract

ADAM family plays important roles in neurogenesis. The cytoplasmic tail of ADAM19 (ADAM19-CT) contains 193 residues. The presence of two putative SH3 ligand-binding sites suggests potential interactions with cytosolic proteins, which could be possibly linked to the functions of ADAM19. To address these issues, a yeast two-hybrid screen was performed in human fetal brain cDNA library to isolate proteins that interact with the cytoplasmic tail of ADAM19. Four proteins were obtained, ArgBP1, β-cop, ubiquitin and a novel protein. GST-Pulldown assay has confirmed the interaction between AdAM19 and ArgBP1. By constructing series of deletion mutants of ADAM19-CT and ArgBP1 respectively, the interaction regions have been identified. They are the SH3 binding sites in ADAM19-CT and the P4 region in ArgBP1. And the interaction is specific. ArgBP1 does not bind to ADAM22, ADAM29 or ADAM9 (mouse). ArgBP1may be the key protein, which accounts for the physiological function of ADAM19.

Original language	English (US)
Pages (from-to)	317-323
Number of pages	7
Journal	Molecular Biology Reports
Volume	29
Issue number	3
DOIs	https://doi.org/10.1023/A:1020409217215
State	Published - Sep 2002
Externally published	Yes

Keywords

ADAM
ArgBP1
Yeast two-hybrid

ASJC Scopus subject areas

Molecular Biology
Genetics

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10.1023/A:1020409217215

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Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., Davis, N., Dicks, E., Ewing, R., Floyd, Y., Gray, K., Hall, S., Hawes, R., Hughes, J., Kosmidou, V., ... Futreal, P. A. (2002). Screen and identification of proteins interacting with ADAM19 cytoplasmic tail. Molecular Biology Reports, 29(3), 317-323. https://doi.org/10.1023/A:1020409217215

Davies, H, Bignell, GR, Cox, C, Stephens, P, Edkins, S, Clegg, S, Teague, J, Woffendin, H, Garnett, MJ, Bottomley, W, Davis, N, Dicks, E, Ewing, R, Floyd, Y, Gray, K, Hall, S, Hawes, R, Hughes, J, Kosmidou, V, Menzies, A, Mould, C, Parker, A, Stevens, C, Watt, S, Hooper, S, Jayatilake, H, Gusterson, BA, Cooper, C, Shipley, J, Hargrave, D, Pritchard-Jones, K, Maitland, N, Chenevix-Trench, G, Riggins, GJ, Bigner, DD, Palmieri, G, Cossu, A, Flanagan, A, Nicholson, A, Ho, JWC, Leung, SY, Yuen, ST, Weber, BL, Seigler, HF, Darrow, TL, Paterson, H, Wooster, R, Stratton, MR & Futreal, PA 2002, 'Screen and identification of proteins interacting with ADAM19 cytoplasmic tail', Molecular Biology Reports, vol. 29, no. 3, pp. 317-323. https://doi.org/10.1023/A:1020409217215

@article{65eb3e34a6cd44b399847e6a8469b676,

title = "Screen and identification of proteins interacting with ADAM19 cytoplasmic tail",

abstract = "ADAM family plays important roles in neurogenesis. The cytoplasmic tail of ADAM19 (ADAM19-CT) contains 193 residues. The presence of two putative SH3 ligand-binding sites suggests potential interactions with cytosolic proteins, which could be possibly linked to the functions of ADAM19. To address these issues, a yeast two-hybrid screen was performed in human fetal brain cDNA library to isolate proteins that interact with the cytoplasmic tail of ADAM19. Four proteins were obtained, ArgBP1, β-cop, ubiquitin and a novel protein. GST-Pulldown assay has confirmed the interaction between AdAM19 and ArgBP1. By constructing series of deletion mutants of ADAM19-CT and ArgBP1 respectively, the interaction regions have been identified. They are the SH3 binding sites in ADAM19-CT and the P4 region in ArgBP1. And the interaction is specific. ArgBP1 does not bind to ADAM22, ADAM29 or ADAM9 (mouse). ArgBP1may be the key protein, which accounts for the physiological function of ADAM19.",

keywords = "ADAM, ArgBP1, Yeast two-hybrid",

author = "Helen Davies and Bignell, {Graham R.} and Charles Cox and Philip Stephens and Sarah Edkins and Sheila Clegg and Jon Teague and Hayley Woffendin and Garnett, {Mathew J.} and William Bottomley and Neil Davis and Ed Dicks and Rebecca Ewing and Yvonne Floyd and Kristian Gray and Sarah Hall and Rachel Hawes and Jaime Hughes and Vivian Kosmidou and Andrew Menzies and Catherine Mould and Adrian Parker and Claire Stevens and Stephen Watt and Steven Hooper and Hiran Jayatilake and Gusterson, {Barry A.} and Colin Cooper and Janet Shipley and Darren Hargrave and Katherine Pritchard-Jones and Norman Maitland and Georgia Chenevix-Trench and Riggins, {Gregory J.} and Bigner, {Darell D.} and Giuseppe Palmieri and Antonio Cossu and Adrienne Flanagan and Andrew Nicholson and Ho, {Judy W.C.} and Leung, {Suet Y.} and Yuen, {Siu T.} and Weber, {Barbara L.} and Seigler, {Hilliard F.} and Darrow, {Timothy L.} and Hugh Paterson and Richard Wooster and Stratton, {Michael R.} and Futreal, {P. Andrew}",

note = "Funding Information: We thank Dr Tongwen Wang for providing Yeast strain S. cerevisiae EGY48. We also wish to thank all the colleagues for valuable advice. This work was supported by National Natural Science Foundation of China, grant No. 30170866.",

year = "2002",

month = sep,

doi = "10.1023/A:1020409217215",

language = "English (US)",

volume = "29",

pages = "317--323",

journal = "Molecular Biology Reports",

issn = "0301-4851",

publisher = "Springer Netherlands",

number = "3",

}

TY - JOUR

T1 - Screen and identification of proteins interacting with ADAM19 cytoplasmic tail

AU - Davies, Helen

AU - Bignell, Graham R.

AU - Cox, Charles

AU - Stephens, Philip

AU - Edkins, Sarah

AU - Clegg, Sheila

AU - Teague, Jon

AU - Woffendin, Hayley

AU - Garnett, Mathew J.

AU - Bottomley, William

AU - Davis, Neil

AU - Dicks, Ed

AU - Ewing, Rebecca

AU - Floyd, Yvonne

AU - Gray, Kristian

AU - Hall, Sarah

AU - Hawes, Rachel

AU - Hughes, Jaime

AU - Kosmidou, Vivian

AU - Menzies, Andrew

AU - Mould, Catherine

AU - Parker, Adrian

AU - Stevens, Claire

AU - Watt, Stephen

AU - Hooper, Steven

AU - Jayatilake, Hiran

AU - Gusterson, Barry A.

AU - Cooper, Colin

AU - Shipley, Janet

AU - Hargrave, Darren

AU - Pritchard-Jones, Katherine

AU - Maitland, Norman

AU - Chenevix-Trench, Georgia

AU - Riggins, Gregory J.

AU - Bigner, Darell D.

AU - Palmieri, Giuseppe

AU - Cossu, Antonio

AU - Flanagan, Adrienne

AU - Nicholson, Andrew

AU - Ho, Judy W.C.

AU - Leung, Suet Y.

AU - Yuen, Siu T.

AU - Weber, Barbara L.

AU - Seigler, Hilliard F.

AU - Darrow, Timothy L.

AU - Paterson, Hugh

AU - Wooster, Richard

AU - Stratton, Michael R.

AU - Futreal, P. Andrew

N1 - Funding Information: We thank Dr Tongwen Wang for providing Yeast strain S. cerevisiae EGY48. We also wish to thank all the colleagues for valuable advice. This work was supported by National Natural Science Foundation of China, grant No. 30170866.

PY - 2002/9

Y1 - 2002/9

N2 - ADAM family plays important roles in neurogenesis. The cytoplasmic tail of ADAM19 (ADAM19-CT) contains 193 residues. The presence of two putative SH3 ligand-binding sites suggests potential interactions with cytosolic proteins, which could be possibly linked to the functions of ADAM19. To address these issues, a yeast two-hybrid screen was performed in human fetal brain cDNA library to isolate proteins that interact with the cytoplasmic tail of ADAM19. Four proteins were obtained, ArgBP1, β-cop, ubiquitin and a novel protein. GST-Pulldown assay has confirmed the interaction between AdAM19 and ArgBP1. By constructing series of deletion mutants of ADAM19-CT and ArgBP1 respectively, the interaction regions have been identified. They are the SH3 binding sites in ADAM19-CT and the P4 region in ArgBP1. And the interaction is specific. ArgBP1 does not bind to ADAM22, ADAM29 or ADAM9 (mouse). ArgBP1may be the key protein, which accounts for the physiological function of ADAM19.

AB - ADAM family plays important roles in neurogenesis. The cytoplasmic tail of ADAM19 (ADAM19-CT) contains 193 residues. The presence of two putative SH3 ligand-binding sites suggests potential interactions with cytosolic proteins, which could be possibly linked to the functions of ADAM19. To address these issues, a yeast two-hybrid screen was performed in human fetal brain cDNA library to isolate proteins that interact with the cytoplasmic tail of ADAM19. Four proteins were obtained, ArgBP1, β-cop, ubiquitin and a novel protein. GST-Pulldown assay has confirmed the interaction between AdAM19 and ArgBP1. By constructing series of deletion mutants of ADAM19-CT and ArgBP1 respectively, the interaction regions have been identified. They are the SH3 binding sites in ADAM19-CT and the P4 region in ArgBP1. And the interaction is specific. ArgBP1 does not bind to ADAM22, ADAM29 or ADAM9 (mouse). ArgBP1may be the key protein, which accounts for the physiological function of ADAM19.

KW - ADAM

KW - ArgBP1

KW - Yeast two-hybrid

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U2 - 10.1023/A:1020409217215

DO - 10.1023/A:1020409217215

M3 - Article

C2 - 12463424

AN - SCOPUS:0036710510

SN - 0301-4851

VL - 29

SP - 317

EP - 323

JO - Molecular Biology Reports

JF - Molecular Biology Reports

IS - 3

ER -

Screen and identification of proteins interacting with ADAM19 cytoplasmic tail

Abstract

Keywords

ASJC Scopus subject areas

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