Intracellular and extracellular control of activin function by novel regulatory molecules

Kunihiro Tsuchida, Takashi Matsuzaki, Norio Yamakawa, Zhong Hui Liu, Hiromu Sugino

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Activin signal transduction is regulated through multiple mechanisms. We have identified novel regulatory proteins that control activin functions either intracellularly or extracellularly. As intracellular molecules, PSD-95/Dlg/ZO-1 (PDZ) proteins that specifically associate with activin type II receptors (ActRIIs) were identified. We have named the molecules as activin receptor-interacting proteins (ARIPs). ARIP1 has two WW domains and five PDZ domains, associates not only with ActRIIs but also with Smads, and controls activin functions intracellularly in neuronal cells. Another ARIP we have found has only one PDZ domain, and is likely to be involved in intracellular trafficking and sorting of activin receptor complexes in the cell. As an extracellular regulatory protein, we have identified a novel follistatin-like protein, named follistatin-related gene (FLRG). Like follistatins, FLRG binds activins and bone morphogenetic proteins (BMPs) and controls their functions extracellularly. The mode of association of follistatin and FLRG with activins and their expression patterns are different, suggesting the distinct functions of follistatin and FLRG in vivo.

Original languageEnglish
Pages (from-to)25-31
Number of pages7
JournalMolecular and Cellular Endocrinology
Volume180
Issue number1-2
DOIs
Publication statusPublished - 30-07-2001

Fingerprint

Follistatin
Activins
Activin Receptors
Molecules
Receptor-Interacting Protein Serine-Threonine Kinases
Genes
Follistatin-Related Proteins
Type II Activin Receptors
Proteins
Bone Morphogenetic Proteins
Signal transduction
Sorting
Signal Transduction
Association reactions

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Endocrinology

Cite this

Tsuchida, Kunihiro ; Matsuzaki, Takashi ; Yamakawa, Norio ; Liu, Zhong Hui ; Sugino, Hiromu. / Intracellular and extracellular control of activin function by novel regulatory molecules. In: Molecular and Cellular Endocrinology. 2001 ; Vol. 180, No. 1-2. pp. 25-31.
@article{b1bbc546491d4c64815c36c22f9a0baf,
title = "Intracellular and extracellular control of activin function by novel regulatory molecules",
abstract = "Activin signal transduction is regulated through multiple mechanisms. We have identified novel regulatory proteins that control activin functions either intracellularly or extracellularly. As intracellular molecules, PSD-95/Dlg/ZO-1 (PDZ) proteins that specifically associate with activin type II receptors (ActRIIs) were identified. We have named the molecules as activin receptor-interacting proteins (ARIPs). ARIP1 has two WW domains and five PDZ domains, associates not only with ActRIIs but also with Smads, and controls activin functions intracellularly in neuronal cells. Another ARIP we have found has only one PDZ domain, and is likely to be involved in intracellular trafficking and sorting of activin receptor complexes in the cell. As an extracellular regulatory protein, we have identified a novel follistatin-like protein, named follistatin-related gene (FLRG). Like follistatins, FLRG binds activins and bone morphogenetic proteins (BMPs) and controls their functions extracellularly. The mode of association of follistatin and FLRG with activins and their expression patterns are different, suggesting the distinct functions of follistatin and FLRG in vivo.",
author = "Kunihiro Tsuchida and Takashi Matsuzaki and Norio Yamakawa and Liu, {Zhong Hui} and Hiromu Sugino",
year = "2001",
month = "7",
day = "30",
doi = "10.1016/S0303-7207(01)00522-6",
language = "English",
volume = "180",
pages = "25--31",
journal = "Molecular and Cellular Endocrinology",
issn = "0303-7207",
publisher = "Elsevier Ireland Ltd",
number = "1-2",

}

Intracellular and extracellular control of activin function by novel regulatory molecules. / Tsuchida, Kunihiro; Matsuzaki, Takashi; Yamakawa, Norio; Liu, Zhong Hui; Sugino, Hiromu.

In: Molecular and Cellular Endocrinology, Vol. 180, No. 1-2, 30.07.2001, p. 25-31.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Intracellular and extracellular control of activin function by novel regulatory molecules

AU - Tsuchida, Kunihiro

AU - Matsuzaki, Takashi

AU - Yamakawa, Norio

AU - Liu, Zhong Hui

AU - Sugino, Hiromu

PY - 2001/7/30

Y1 - 2001/7/30

N2 - Activin signal transduction is regulated through multiple mechanisms. We have identified novel regulatory proteins that control activin functions either intracellularly or extracellularly. As intracellular molecules, PSD-95/Dlg/ZO-1 (PDZ) proteins that specifically associate with activin type II receptors (ActRIIs) were identified. We have named the molecules as activin receptor-interacting proteins (ARIPs). ARIP1 has two WW domains and five PDZ domains, associates not only with ActRIIs but also with Smads, and controls activin functions intracellularly in neuronal cells. Another ARIP we have found has only one PDZ domain, and is likely to be involved in intracellular trafficking and sorting of activin receptor complexes in the cell. As an extracellular regulatory protein, we have identified a novel follistatin-like protein, named follistatin-related gene (FLRG). Like follistatins, FLRG binds activins and bone morphogenetic proteins (BMPs) and controls their functions extracellularly. The mode of association of follistatin and FLRG with activins and their expression patterns are different, suggesting the distinct functions of follistatin and FLRG in vivo.

AB - Activin signal transduction is regulated through multiple mechanisms. We have identified novel regulatory proteins that control activin functions either intracellularly or extracellularly. As intracellular molecules, PSD-95/Dlg/ZO-1 (PDZ) proteins that specifically associate with activin type II receptors (ActRIIs) were identified. We have named the molecules as activin receptor-interacting proteins (ARIPs). ARIP1 has two WW domains and five PDZ domains, associates not only with ActRIIs but also with Smads, and controls activin functions intracellularly in neuronal cells. Another ARIP we have found has only one PDZ domain, and is likely to be involved in intracellular trafficking and sorting of activin receptor complexes in the cell. As an extracellular regulatory protein, we have identified a novel follistatin-like protein, named follistatin-related gene (FLRG). Like follistatins, FLRG binds activins and bone morphogenetic proteins (BMPs) and controls their functions extracellularly. The mode of association of follistatin and FLRG with activins and their expression patterns are different, suggesting the distinct functions of follistatin and FLRG in vivo.

UR - http://www.scopus.com/inward/record.url?scp=0035974509&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0035974509&partnerID=8YFLogxK

U2 - 10.1016/S0303-7207(01)00522-6

DO - 10.1016/S0303-7207(01)00522-6

M3 - Article

C2 - 11451568

AN - SCOPUS:0035974509

VL - 180

SP - 25

EP - 31

JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

SN - 0303-7207

IS - 1-2

ER -