Affiliations: Structural Genomics Section, Saha Institute of Nuclear Physics, 1/AF Bidhan Nagar, Kolkata 700 064, India
Correspondence:
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Corresponding author: Debashis Mukhopadhyay, Ph.D., Structural Genomics Section, Saha Institute of Nuclear Physics, 1/AF Bidhan Nagar, Kolkata 700 064, India. Tel.: +91 33 2337 5345 49; Fax: +91 33 2337 4637; E-mail: debashis.mukhopadhyay@saha.ac.in.
Abstract: In view of the emerging evidence that amyloid-β load in the brain and neuronal deficits are possibly independent events and the increasing importance of downstream molecular cascades in Alzheimer's Disease (AD) pathogenesis, the role of Amyloid Intracellular C-terminal Domain (AICD) is evaluated. This C-terminal fragment of Amyloid-β protein precursor (AβPP) is cytotoxic and is a major component of AD brain. Different portions of AICD bind to different ‘adaptors’ and are seen to take part in various cellular events including AβPP processing and trafficking, apoptosis, neuronal growth and regulation of gene transcription. Phosphorylation also plays an important role in terms of choice of binding partners. The review emphasizes the dynamics of the network created by AICD interactions and points to possible alternative routes of AD like neurodegeneration.
