Ankyrins

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ankyrin 1, erythrocytic
Ribbon diagram of a fragment of the membrane-binding domain of ankyrin 1. From PDB: 1N11​.
Identifiers
SymbolANK1
Alt. symbolsANK
Entrez286
HUGO492
OMIM182900
RefSeqNM_000037
UniProtP16157
Other data
LocusChr. 8 p21.1-11.2
ankyrin 2, neuronal
Identifiers
SymbolANK2
Alt. symbolsLQT4
Entrez287
HUGO493
OMIM106410
RefSeqNM_001148
UniProtQ01484
Other data
LocusChr. 4 q25-q27
ankyrin 3, node of Ranvier (ankyrin G)
Identifiers
SymbolANK3
Entrez288
HUGO494
OMIM600465
RefSeqNM_020987
UniProtQ12955
Other data
LocusChr. 10 q21

Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Associate Editor-In-Chief: Cafer Zorkun, M.D., Ph.D. [2]


Overview

Ankyrins are a family of proteins that mediates the attachment of integral membrane proteins to the cytoskeleton.[1]

Ankyrin 1, was first discovered in the erythrocytes but also later found to be expressed in the brain and muscles. In erythrocytes, Ankyrin 1 links membrane receptor CD44 to inositol triphosphate and the cytoskeleton.[2]

Ankyrin contains three functional domains: a conserved N-terminal ankyrin repeat domain (ARD) consisting of 22–24 tandem repeats of 33 amino acids, a spectrin binding domain and a variably sized C-terminal regulatory domain.

Ankyrin was discovered by Dr. G. Vann Bennett (M.D., PhD.) in 1976.

References

  1. Hryniewicz-Jankowska A, Czogalla A, Bok E, Sikorsk AF (2002). "Ankyrins, multifunctional proteins involved in many cellular pathways". Folia Histochem Cytobiol. 40 (3): 239–49. PMID 12219834.
  2. Singleton PA, Bourguignon LY (2004). "CD44 interaction with ankyrin and IP3 receptor in lipid rafts promotes hyaluronan-mediated Ca2+ signaling leading to nitric oxide production and endothelial cell adhesion and proliferation". Exp Cell Res. 295 (1): 102–18. PMID 15051494.

External links


de:Ankyrin


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