Actinin: Difference between revisions
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'''Actinin''' is a [[microfilament]] protein. [[ACTN1|α-Actinin]] is necessary for the attachment of [[actin]] filaments to the [[Sarcomere|Z-line]]s in [[Skeletal muscle|skeletal muscle cells]], and to the [[Smooth muscle tissue|dense bodies]] in [[smooth muscle cells]]. The functional protein is an anti-parallel [[protein dimer|dimer]], which cross-links the thin filaments in adjacent [[sarcomeres]], and therefore coordinated contractions between sarcomeres in the horizontal axis. |
'''Actinin''' is a [[microfilament]] protein. [[ACTN1|α-Actinin]] is necessary for the attachment of [[actin]] filaments to the [[Sarcomere|Z-line]]s in [[Skeletal muscle|skeletal muscle cells]]<ref>{{cite book|title=Ganong's Review of Medical Physiology, 24th Edition|year=2012|publisher=Lange (Tata McGraw Hill)|page=100}}</ref> , and to the [[Smooth muscle tissue|dense bodies]] in [[smooth muscle cells]]. The functional protein is an anti-parallel [[protein dimer|dimer]], which cross-links the thin filaments in adjacent [[sarcomeres]], and therefore coordinated contractions between sarcomeres in the horizontal axis. |
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The non-sarcomeric α-actinins (ACTN1 and ACTN4) are widely expressed. Both ends of the rod-shaped α-actinin dimer contain actin-binding domains. |
The non-sarcomeric α-actinins (ACTN1 and ACTN4) are widely expressed. Both ends of the rod-shaped α-actinin dimer contain actin-binding domains. |
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* [[actin]] |
* [[actin]] |
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==References== |
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{{reflist}} |
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==External links== |
==External links== |
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* {{MeshName|Actinin}} |
* {{MeshName|Actinin}} |
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Revision as of 08:44, 3 January 2014
Actinin is a microfilament protein. α-Actinin is necessary for the attachment of actin filaments to the Z-lines in skeletal muscle cells[1] , and to the dense bodies in smooth muscle cells. The functional protein is an anti-parallel dimer, which cross-links the thin filaments in adjacent sarcomeres, and therefore coordinated contractions between sarcomeres in the horizontal axis.
The non-sarcomeric α-actinins (ACTN1 and ACTN4) are widely expressed. Both ends of the rod-shaped α-actinin dimer contain actin-binding domains.
Mutations in ACTN4 can cause the kidney disease focal segmental glomerulosclerosis.
Genes
See also
References
- ^ Ganong's Review of Medical Physiology, 24th Edition. Lange (Tata McGraw Hill). 2012. p. 100.
External links
- Actinin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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