Journal
JOURNAL OF CELLULAR AND MOLECULAR MEDICINE
Volume 13, Issue 11-12, Pages 4364-4376Publisher
WILEY
DOI: 10.1111/j.1582-4934.2009.00943.x
Keywords
ankyrin; beta-spectrin; obscurin; L1-CAM; cardiomyocyte; axon initial segment; node of Ranvier
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Funding
- NIH [HL084583, HL083422, HL092232]
- Pew Scholars Trust
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Introduction Ankyrin Ankyrin functional domains Ankyrin genes, alternative splicing and the diversity of ankyrin polypeptides Mechanisms that target and stabilize ankyrin beta-spectrin L1-cell adhesion molecules Obscurin Ankyrins and disease Ankyrin-R Ankyrin-G Ankyrin-B Conclusion In eukaryotic cells, ankyrins serve as adaptor proteins that link membrane proteins to the underlying cytoskeleton. These adaptor proteins form protein complexes consisting of integral membrane proteins, signalling molecules and cytoskeletal components. With their modular architecture and ability to interact with many proteins, ankyrins organize and stabilize these protein networks, thereby establishing the infrastructure of membrane domains with specialized functions. To this end, ankyrin collaborates with a number of proteins including cytoskeletal proteins, cell adhesion molecules and large structural proteins. This review addresses the targeting and stabilization of protein networks related to ankyrin interactions with the cytoskeletal protein beta-spectrin, L1-cell adhesion molecules and the large myofibrillar protein obscurin. The significance of these interactions for differential targeting of cardiac proteins and neuronal membrane formation is also presented. Finally, this review concludes with a discussion about ankyrin dysfunction in human diseases such as haemolytic anaemia, cardiac arrhythmia and neurological disorders.
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