Isolation and characterization of AINT: A novel ARNT interacting protein expressed during murine embryonic development

Christine M. Sadek; Stéphan Jalaguier; Eimear P. Feeney; Marjo Aitola; Anastasios E. Damdimopoulos; Markku Pelto-Huikko; Jan Åke Gustafsson

doi:10.1016/S0925-4773(00)00415-9

Isolation and characterization of AINT: A novel ARNT interacting protein expressed during murine embryonic development

Christine M. Sadek, Stéphan Jalaguier, Eimear P. Feeney, Marjo Aitola, Anastasios E. Damdimopoulos, Markku Pelto-Huikko, Jan Åke Gustafsson

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

66 Scopus citations

Abstract

Basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) proteins form dimeric transcription factors to mediate diverse biological functions including xenobiotic metabolism, hypoxic response, circadian rhythm and central nervous system midline development. The Ah receptor nuclear translocator protein (ARNT) plays a central role as a common heterodimerization partner. Herein, we describe a novel, embryonically expressed, ARNT interacting protein (AINT) that may be a member of a larger coiled-coil PAS interacting protein family. The AINT C-terminus mediates interaction with the PAS domain of ARNT in yeast and interacts in vitro with ARNT and ARNT2 specifically. AINT localizes to the cytoplasm and overexpression leads to non-nuclear localization of ARNT. A dynamic pattern of AINT mRNA expression during embryogenesis and cerebellum ontogeny supports a role for AINT in development. (C) 2000 Elsevier Science Ireland Ltd.

Original language	English (US)
Pages (from-to)	13-26
Number of pages	14
Journal	Mechanisms of Development
Volume	97
Issue number	1-2
DOIs	https://doi.org/10.1016/S0925-4773(00)00415-9
State	Published - Oct 2000

Keywords

Ah receptor nuclear translocator
ARNT
ARNT2
Basic helix-loop-helix-PAS
bHLH-PAS
Coiled-coil
HIF-1α
HLF
Hypoxia
NPAS
TACC
Yeast two- hybrid

ASJC Scopus subject areas

Developmental Biology
Developmental Neuroscience

Access to Document

10.1016/S0925-4773(00)00415-9

Cite this

@article{b8dcbe93049c47aa9a2e65638d12a466,

title = "Isolation and characterization of AINT: A novel ARNT interacting protein expressed during murine embryonic development",

abstract = "Basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) proteins form dimeric transcription factors to mediate diverse biological functions including xenobiotic metabolism, hypoxic response, circadian rhythm and central nervous system midline development. The Ah receptor nuclear translocator protein (ARNT) plays a central role as a common heterodimerization partner. Herein, we describe a novel, embryonically expressed, ARNT interacting protein (AINT) that may be a member of a larger coiled-coil PAS interacting protein family. The AINT C-terminus mediates interaction with the PAS domain of ARNT in yeast and interacts in vitro with ARNT and ARNT2 specifically. AINT localizes to the cytoplasm and overexpression leads to non-nuclear localization of ARNT. A dynamic pattern of AINT mRNA expression during embryogenesis and cerebellum ontogeny supports a role for AINT in development. (C) 2000 Elsevier Science Ireland Ltd.",

keywords = "Ah receptor nuclear translocator, ARNT, ARNT2, Basic helix-loop-helix-PAS, bHLH-PAS, Coiled-coil, HIF-1α, HLF, Hypoxia, NPAS, TACC, Yeast two- hybrid",

author = "Sadek, {Christine M.} and St{\'e}phan Jalaguier and Feeney, {Eimear P.} and Marjo Aitola and Damdimopoulos, {Anastasios E.} and Markku Pelto-Huikko and Gustafsson, {Jan {\AA}ke}",

note = "Funding Information: Our sincere thanks to E. Flinn, G. Schuster, J. Thomsen, M. Tujague, W. Fossman and B.L. Allen-Hoffmann for critical reading of the manuscript, to C.A. Bradfield, P. Moffett, J. Pelletier, L. Poellinger and M.C. Simon for supplying plasmids necessary for these studies, to U. Jukarainen for skillful technical help, to C. Rowlands and W. Wilson for assistance in the early stages of this project and to the Mammalian Embryo and Genome Core Facility at Karolinska Institute. This work was supported by the Swedish Cancer Society and the Research Fund of Tampere University Hospital.",

year = "2000",

month = oct,

doi = "10.1016/S0925-4773(00)00415-9",

language = "English (US)",

volume = "97",

pages = "13--26",

journal = "Mechanisms of Development",

issn = "0925-4773",

publisher = "John Wiley & Sons Inc.",

number = "1-2",

}

TY - JOUR

T1 - Isolation and characterization of AINT

T2 - A novel ARNT interacting protein expressed during murine embryonic development

AU - Sadek, Christine M.

AU - Jalaguier, Stéphan

AU - Feeney, Eimear P.

AU - Aitola, Marjo

AU - Damdimopoulos, Anastasios E.

AU - Pelto-Huikko, Markku

AU - Gustafsson, Jan Åke

N1 - Funding Information: Our sincere thanks to E. Flinn, G. Schuster, J. Thomsen, M. Tujague, W. Fossman and B.L. Allen-Hoffmann for critical reading of the manuscript, to C.A. Bradfield, P. Moffett, J. Pelletier, L. Poellinger and M.C. Simon for supplying plasmids necessary for these studies, to U. Jukarainen for skillful technical help, to C. Rowlands and W. Wilson for assistance in the early stages of this project and to the Mammalian Embryo and Genome Core Facility at Karolinska Institute. This work was supported by the Swedish Cancer Society and the Research Fund of Tampere University Hospital.

PY - 2000/10

Y1 - 2000/10

N2 - Basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) proteins form dimeric transcription factors to mediate diverse biological functions including xenobiotic metabolism, hypoxic response, circadian rhythm and central nervous system midline development. The Ah receptor nuclear translocator protein (ARNT) plays a central role as a common heterodimerization partner. Herein, we describe a novel, embryonically expressed, ARNT interacting protein (AINT) that may be a member of a larger coiled-coil PAS interacting protein family. The AINT C-terminus mediates interaction with the PAS domain of ARNT in yeast and interacts in vitro with ARNT and ARNT2 specifically. AINT localizes to the cytoplasm and overexpression leads to non-nuclear localization of ARNT. A dynamic pattern of AINT mRNA expression during embryogenesis and cerebellum ontogeny supports a role for AINT in development. (C) 2000 Elsevier Science Ireland Ltd.

AB - Basic helix-loop-helix-PER-ARNT-SIM (bHLH-PAS) proteins form dimeric transcription factors to mediate diverse biological functions including xenobiotic metabolism, hypoxic response, circadian rhythm and central nervous system midline development. The Ah receptor nuclear translocator protein (ARNT) plays a central role as a common heterodimerization partner. Herein, we describe a novel, embryonically expressed, ARNT interacting protein (AINT) that may be a member of a larger coiled-coil PAS interacting protein family. The AINT C-terminus mediates interaction with the PAS domain of ARNT in yeast and interacts in vitro with ARNT and ARNT2 specifically. AINT localizes to the cytoplasm and overexpression leads to non-nuclear localization of ARNT. A dynamic pattern of AINT mRNA expression during embryogenesis and cerebellum ontogeny supports a role for AINT in development. (C) 2000 Elsevier Science Ireland Ltd.

KW - Ah receptor nuclear translocator

KW - ARNT

KW - ARNT2

KW - Basic helix-loop-helix-PAS

KW - bHLH-PAS

KW - Coiled-coil

KW - HIF-1α

KW - HLF

KW - Hypoxia

KW - NPAS

KW - TACC

KW - Yeast two- hybrid

UR - http://www.scopus.com/inward/record.url?scp=0343278978&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0343278978&partnerID=8YFLogxK

U2 - 10.1016/S0925-4773(00)00415-9

DO - 10.1016/S0925-4773(00)00415-9

M3 - Article

C2 - 11025203

AN - SCOPUS:0343278978

SN - 0925-4773

VL - 97

SP - 13

EP - 26

JO - Mechanisms of Development

JF - Mechanisms of Development

IS - 1-2

ER -

Isolation and characterization of AINT: A novel ARNT interacting protein expressed during murine embryonic development

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this