Actinin

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.^[2] The functional protein is an anti-parallel dimer, which cross-links the thin filaments in adjacent sarcomeres, and therefore coordinates contractions between sarcomeres in the horizontal axis.

The non-sarcomeric α-actinins, encoded by ACTN1 and ACTN4, are widely expressed. ACTN2 expression is found in both cardiac and skeletal muscle, whereas ACTN3 is limited to the latter. Both ends of the rod-shaped α-actinin dimer contain actin-binding domains.

Mutations in ACTN4 can cause the kidney disease focal segmental glomerulosclerosis (FSGS).^[3]

References[]

^ Ganong's Review of Medical Physiology, 24th Edition. Lange (Tata McGraw Hill). 2012. p. 100.
^ Laszlo Szekeres; Julius G. Papp (6 December 2012). Pharmacology of Smooth Muscle. Springer Science & Business Media. pp. 17–18. ISBN 978-3-642-78920-5.
^ Richard P. Lifton; Stefan Somlo; Gerhard H. Giebisch; Donald W. Seldin (25 February 2009). Genetic Diseases of the Kidney. Academic Press. pp. 117–118. ISBN 978-0-08-092427-4.

External links[]

Actinin at the US National Library of Medicine Medical Subject Headings (MeSH)

This protein-related article is a stub. You can help Wikipedia by .

[1] Ganong's Review of Medical Physiology, 24th Edition. Lange (Tata McGraw Hill). 2012. p. 100.

[SzekeresPapp2012-2] Laszlo Szekeres; Julius G. Papp (6 December 2012). Pharmacology of Smooth Muscle. Springer Science & Business Media. pp. 17–18. ISBN 978-3-642-78920-5.

[LiftonSomlo2009-3] Richard P. Lifton; Stefan Somlo; Gerhard H. Giebisch; Donald W. Seldin (25 February 2009). Genetic Diseases of the Kidney. Academic Press. pp. 117–118. ISBN 978-0-08-092427-4.

[1]

[2]

[3]

Actinin

See also[]

References[]

External links[]