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Tetraspan proteins: regulators of renal structure and function.
- Source :
-
Current opinion in nephrology and hypertension [Curr Opin Nephrol Hypertens] 2007 Jul; Vol. 16 (4), pp. 353-8. - Publication Year :
- 2007
-
Abstract
- Purpose of Review: Members of the tetraspan family are widely expressed and poorly understood. An emerging literature suggests that through their interactions with other membrane proteins they play central or regulatory roles in a wide variety of physiological processes. This review will discuss selected tetraspan complexes and highlight their relevance to epithelial cells and the kidney.<br />Recent Findings: Tetraspans regulate the signaling and trafficking properties of their partner proteins. Tetraspan complexes with integrin molecules, for example, modulate cell adhesion and mobility. Perturbations of tetraspan-integrin assemblies can have dramatic impacts on renal tissue morphogenesis, resulting in a disruption of normal glomerular architecture and selectivity. Tetraspan interactions with renal ion transport proteins appear to affect transporter function by enhancing or inhibiting the endocytic internalization of their transport protein partners.<br />Summary: Tetraspans constitute a novel class of proteins whose capacity to alter the cell biological and functional properties of their membrane protein partners is likely to have wide ranging and important physiological ramifications.
- Subjects :
- Animals
Epithelial Cells physiology
H(+)-K(+)-Exchanging ATPase metabolism
Humans
Immune System physiology
Integrins physiology
Kidney Glomerulus anatomy & histology
Kidney Glomerulus drug effects
Membrane Glycoproteins physiology
Platelet Membrane Glycoproteins physiology
Protein Transport drug effects
Tetraspanin 24
Tetraspanin 28
Tetraspanin 29
Tetraspanin 30
Antigens, CD physiology
Kidney physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1062-4821
- Volume :
- 16
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Current opinion in nephrology and hypertension
- Publication Type :
- Academic Journal
- Accession number :
- 17565278
- Full Text :
- https://doi.org/10.1097/MNH.0b013e328177b1fa