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Gene Review:

Ahnak - AHNAK nucleoprotein

Rattus norvegicus

Synonyms: AHNAK 1, RGD1308572, UV118

Borgonovo, B. et al., Alvarez, J. et al., Haase, H. et al., Haase, H. et al., Sköldberg, F. et al.

Sköldberg, Rönnblom, Thornemo, Lindahl, Bird, Rorsman, Kämpe, Landgren,

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Disease relevance of Ahnak

This is the first report that AHNAK can be targeted by the immune system in autoimmune disease [1].

Psychiatry related information on Ahnak

This genetic ahnak variant might cause individual differences in I(CaL) regulation upon physiological challenges or therapeutic interventions [2].

High impact information on Ahnak

We have now identified a marker of the process, desmoyokin-AHNAK, in a clonal derivative of the neuronal cell line, PC12 [3].
Desmoyokin-AHNAK-positive vesicles exist in a variety of cells and tissues and are distinct from the endoplasmic reticulum, Golgi, trans-Golgi, endosomes and lysosomes, and from Glut4 and constitutive secretion vesicles [3].
In the presence of carboxyl-terminal ahnak protein fragments, isoprenaline induced a similar relative increase in current amplitude and shift in current kinetics [4].
The actin-stabilizing agents, phalloidin and jasplakinolide, did not modify the effects of these ahnak protein fragments on calcium current in control conditions nor in the presence of isoprenaline [4].
Recently, we defined the binding sites among the protein partners in the carboxyl-terminal domain of ahnak [4].

Biological context of Ahnak

The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction [5].

Anatomical context of Ahnak

No endogenous myofibrillar ahnak fragment was observed in the skeletal muscle [5].
We elucidated the role of the recombinant carboxyl-terminal ahnak fragment (ahnak-C2) in actin filament organization and in the function of muscle fibers [5].

References

Identification of AHNAK as a novel autoantigen in systemic lupus erythematosus. Sköldberg, F., Rönnblom, L., Thornemo, M., Lindahl, A., Bird, P.I., Rorsman, F., Kämpe, O., Landgren, E. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
Ahnak is critical for cardiac Ca(V)1.2 calcium channel function and its beta-adrenergic regulation. Haase, H., Alvarez, J., Petzhold, D., Doller, A., Behlke, J., Erdmann, J., Hetzer, R., Regitz-Zagrosek, V., Vassort, G., Morano, I. FASEB J. (2005) [Pubmed]
Regulated exocytosis: a novel, widely expressed system. Borgonovo, B., Cocucci, E., Racchetti, G., Podini, P., Bachi, A., Meldolesi, J. Nat. Cell Biol. (2002) [Pubmed]
Calcium current in rat cardiomyocytes is modulated by the carboxyl-terminal ahnak domain. Alvarez, J., Hamplova, J., Hohaus, A., Morano, I., Haase, H., Vassort, G. J. Biol. Chem. (2004) [Pubmed]
The carboxyl-terminal ahnak domain induces actin bundling and stabilizes muscle contraction. Haase, H., Pagel, I., Khalina, Y., Zacharzowsky, U., Person, V., Lutsch, G., Petzhold, D., Kott, M., Schaper, J., Morano, I. FASEB J. (2004) [Pubmed]

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