Identification and characterization of a PDZ protein that interacts with activin type II receptors

Hiroki Shoji, Kunihiro Tsuchida, Hisashi Kishi, Norio Yamakawa, Takashi Matsuzaki, Zhong Hui Liu, Takanori Nakamura, Hiromu Sugino

Research output: Contribution to journalArticle

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Abstract

We have identified a mouse PDZ protein that interacts with the activin type IIA receptor (ActRIIA), which we named activin receptor-interacting protein 1 (ARIP1). By using yeast two-hybrid screening, we isolated a cDNA clone of ARIP1 from a mouse brain cDNA library. We detected two forms of ARIP1, ARIP1-long and ARIP1-short, which may be produced by alternative splicing. ARIP1-long had one guanylate kinase domain in the NH2-terminal region, followed by two WW domains and five PDZ domains (PDZ1-5). ARIP1-short had a deletion in the NH2-terminal region and lacked the guanylate kinase domain. Both forms interacted with ActRIIA through PDZ5. The COOH-terminal residues of ActRIIA (ESSL) agree with a PDZ-binding consensus motif, and ARIP1 recognized the consensus sequence. ARIP1 interacts specifically with ActRIIA among the receptors for the transforming growth factor β family. Interestingly, ARIP1 also interacted with Smad3, which is an activin/transforming growth factor β intracellular signaling molecule. The mRNA of ARIP1 was more abundant in the brain than in other tissues. Overexpression of ARIP1 controls activin-induced and Smad3-induced transcription in activin-responsive cell lines. These findings suggest that ARIP1 has a significant role in assembling activin signaling molecules at specific subcellular sites and in regulating signal transduction in neuronal cells.

Original languageEnglish
Pages (from-to)5485-5492
Number of pages8
JournalJournal of Biological Chemistry
Volume275
Issue number8
DOIs
Publication statusPublished - 25-02-2000

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Type II Activin Receptors
Activin Receptors
Receptor-Interacting Protein Serine-Threonine Kinases
Activins
Proteins
Guanylate Kinases
Transforming Growth Factors
Brain
PDZ Domains
Signal transduction
Molecules
Consensus Sequence
Alternative Splicing
Gene Library

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Shoji, Hiroki ; Tsuchida, Kunihiro ; Kishi, Hisashi ; Yamakawa, Norio ; Matsuzaki, Takashi ; Liu, Zhong Hui ; Nakamura, Takanori ; Sugino, Hiromu. / Identification and characterization of a PDZ protein that interacts with activin type II receptors. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 8. pp. 5485-5492.
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Shoji, H, Tsuchida, K, Kishi, H, Yamakawa, N, Matsuzaki, T, Liu, ZH, Nakamura, T & Sugino, H 2000, 'Identification and characterization of a PDZ protein that interacts with activin type II receptors', Journal of Biological Chemistry, vol. 275, no. 8, pp. 5485-5492. https://doi.org/10.1074/jbc.275.8.5485

Identification and characterization of a PDZ protein that interacts with activin type II receptors. / Shoji, Hiroki; Tsuchida, Kunihiro; Kishi, Hisashi; Yamakawa, Norio; Matsuzaki, Takashi; Liu, Zhong Hui; Nakamura, Takanori; Sugino, Hiromu.

In: Journal of Biological Chemistry, Vol. 275, No. 8, 25.02.2000, p. 5485-5492.

Research output: Contribution to journalArticle

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AU - Shoji, Hiroki

AU - Tsuchida, Kunihiro

AU - Kishi, Hisashi

AU - Yamakawa, Norio

AU - Matsuzaki, Takashi

AU - Liu, Zhong Hui

AU - Nakamura, Takanori

AU - Sugino, Hiromu

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N2 - We have identified a mouse PDZ protein that interacts with the activin type IIA receptor (ActRIIA), which we named activin receptor-interacting protein 1 (ARIP1). By using yeast two-hybrid screening, we isolated a cDNA clone of ARIP1 from a mouse brain cDNA library. We detected two forms of ARIP1, ARIP1-long and ARIP1-short, which may be produced by alternative splicing. ARIP1-long had one guanylate kinase domain in the NH2-terminal region, followed by two WW domains and five PDZ domains (PDZ1-5). ARIP1-short had a deletion in the NH2-terminal region and lacked the guanylate kinase domain. Both forms interacted with ActRIIA through PDZ5. The COOH-terminal residues of ActRIIA (ESSL) agree with a PDZ-binding consensus motif, and ARIP1 recognized the consensus sequence. ARIP1 interacts specifically with ActRIIA among the receptors for the transforming growth factor β family. Interestingly, ARIP1 also interacted with Smad3, which is an activin/transforming growth factor β intracellular signaling molecule. The mRNA of ARIP1 was more abundant in the brain than in other tissues. Overexpression of ARIP1 controls activin-induced and Smad3-induced transcription in activin-responsive cell lines. These findings suggest that ARIP1 has a significant role in assembling activin signaling molecules at specific subcellular sites and in regulating signal transduction in neuronal cells.

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