Periostin and its interacting proteins in the construction of extracellular architectures

Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (...

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Veröffentlicht in:Cellular and molecular life sciences : CMLS Jg. 74; H. 23; S. 4269 - 4277
Hauptverfasser: Kii, Isao, Ito, Harumi
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Cham Springer International Publishing 01.12.2017
Springer Nature B.V
Schlagworte:
Amino acids
Assembly
Binding sites
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bone Morphogenetic Protein 1 - genetics
Bone Morphogenetic Protein 1 - metabolism
Bone morphogenetic proteins
Cell Adhesion Molecules - genetics
Cell Adhesion Molecules - metabolism
Cell Biology
chemical interactions
collagen
Collagen (type I)
Collagen - genetics
Collagen - metabolism
Connective Tissue - anatomy & histology
Connective Tissue - metabolism
Connective tissues
Construction
Crosslinking
disease course
Electromagnetic interference
enzymes
Extracellular matrix
Fibronectin
fibronectins
Fibronectins - genetics
Fibronectins - metabolism
Gene Expression
Homeostasis
Humans
Laminin
Laminin - genetics
Laminin - metabolism
Life Sciences
Lysyl oxidase
Multi-Author Review
Nephroblastoma Overexpressed Protein - genetics
Nephroblastoma Overexpressed Protein - metabolism
Protein Binding
Protein Interaction Domains and Motifs
Protein Interaction Mapping
Protein Isoforms - genetics
Protein Isoforms - metabolism
Proteins
Proteoglycans - metabolism
Signal Transduction
Tenascin
Tenascin - genetics
Tenascin - metabolism
EMI
FAS 1
Tenascin
Collagen
Fibronectin
BMP-1
ISSN:1420-682X, 1420-9071, 1420-9071
Online-Zugang:Volltext
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Abstract Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (Collagen type I and V, fibronectin, tenascin, and laminin), matricellular proteins (CCN3 and βig-h3), and enzymes that catalyze covalent crosslinking between extracellular matrix proteins (lysyl oxidase and BMP-1). Adjacent binding sites on periostin have been suggested to put the interacting proteins in close proximity, promoting intermolecular interactions between each protein, and leading to their assembly into extracellular architectures. These extracellular architectures determine the mechanochemical properties of connective tissues, in which periostin plays an important role in physiological homeostasis and disease progression. In this review, we introduce the proteins that interact with periostin, and discuss how the multi-domain structure of periostin functions as a scaffold for the assembly of interacting proteins, and how it underlies construction of highly sophisticated extracellular architectures.
AbstractList Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (Collagen type I and V, fibronectin, tenascin, and laminin), matricellular proteins (CCN3 and βig-h3), and enzymes that catalyze covalent crosslinking between extracellular matrix proteins (lysyl oxidase and BMP-1). Adjacent binding sites on periostin have been suggested to put the interacting proteins in close proximity, promoting intermolecular interactions between each protein, and leading to their assembly into extracellular architectures. These extracellular architectures determine the mechanochemical properties of connective tissues, in which periostin plays an important role in physiological homeostasis and disease progression. In this review, we introduce the proteins that interact with periostin, and discuss how the multi-domain structure of periostin functions as a scaffold for the assembly of interacting proteins, and how it underlies construction of highly sophisticated extracellular architectures.
Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (Collagen type I and V, fibronectin, tenascin, and laminin), matricellular proteins (CCN3 and βig-h3), and enzymes that catalyze covalent crosslinking between extracellular matrix proteins (lysyl oxidase and BMP-1). Adjacent binding sites on periostin have been suggested to put the interacting proteins in close proximity, promoting intermolecular interactions between each protein, and leading to their assembly into extracellular architectures. These extracellular architectures determine the mechanochemical properties of connective tissues, in which periostin plays an important role in physiological homeostasis and disease progression. In this review, we introduce the proteins that interact with periostin, and discuss how the multi-domain structure of periostin functions as a scaffold for the assembly of interacting proteins, and how it underlies construction of highly sophisticated extracellular architectures.Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and a carboxyl-terminal domain. These distinct domains have been demonstrated to bind to many proteins including extracellular matrix proteins (Collagen type I and V, fibronectin, tenascin, and laminin), matricellular proteins (CCN3 and βig-h3), and enzymes that catalyze covalent crosslinking between extracellular matrix proteins (lysyl oxidase and BMP-1). Adjacent binding sites on periostin have been suggested to put the interacting proteins in close proximity, promoting intermolecular interactions between each protein, and leading to their assembly into extracellular architectures. These extracellular architectures determine the mechanochemical properties of connective tissues, in which periostin plays an important role in physiological homeostasis and disease progression. In this review, we introduce the proteins that interact with periostin, and discuss how the multi-domain structure of periostin functions as a scaffold for the assembly of interacting proteins, and how it underlies construction of highly sophisticated extracellular architectures.
Author Kii, Isao
Ito, Harumi
Author_xml – sequence: 1
  givenname: Isao
  surname: Kii
  fullname: Kii, Isao
  email: isao.kii@riken.jp
  organization: Common Facilities Unit, Integrated Research Group, Compass to Healthy Life Research Complex Program, RIKEN Cluster for Science and Technology Hub, Pathophysiological and Health Science Team, Imaging Platform and Innovation Group, Division of Bio-Function Dynamics Imaging, RIKEN Center for Life Science Technologies
– sequence: 2
  givenname: Harumi
  surname: Ito
  fullname: Ito, Harumi
  organization: Pathophysiological and Health Science Team, Imaging Platform and Innovation Group, Division of Bio-Function Dynamics Imaging, RIKEN Center for Life Science Technologies
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28887577$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright Springer International Publishing AG 2017
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Snippet Periostin is a matricellular protein that is composed of a multi-domain structure with an amino-terminal EMI domain, a tandem repeat of four FAS 1 domains, and...
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Index Database
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StartPage 4269
SubjectTerms Amino acids
Assembly
Binding sites
Biochemistry
Biomedical and Life Sciences
Biomedicine
Bone Morphogenetic Protein 1 - genetics
Bone Morphogenetic Protein 1 - metabolism
Bone morphogenetic proteins
Cell Adhesion Molecules - genetics
Cell Adhesion Molecules - metabolism
Cell Biology
chemical interactions
collagen
Collagen (type I)
Collagen - genetics
Collagen - metabolism
Connective Tissue - anatomy & histology
Connective Tissue - metabolism
Connective tissues
Construction
Crosslinking
disease course
Electromagnetic interference
enzymes
Extracellular matrix
Fibronectin
fibronectins
Fibronectins - genetics
Fibronectins - metabolism
Gene Expression
Homeostasis
Humans
Laminin
Laminin - genetics
Laminin - metabolism
Life Sciences
Lysyl oxidase
Multi-Author Review
Nephroblastoma Overexpressed Protein - genetics
Nephroblastoma Overexpressed Protein - metabolism
Protein Binding
Protein Interaction Domains and Motifs
Protein Interaction Mapping
Protein Isoforms - genetics
Protein Isoforms - metabolism
Proteins
Proteoglycans - metabolism
Signal Transduction
Tenascin
Tenascin - genetics
Tenascin - metabolism
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Title Periostin and its interacting proteins in the construction of extracellular architectures
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