pdz domain recognition: insight from human tax-interacting protein 1 (tip-1) interaction with target proteins

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ID: 204102
2015
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Abstract
Cellular signaling is primarily directed via protein-protein interactions. PDZ (PSD-95/Discs large/ZO-1 homologous) domains are well known protein-protein interaction modules involved in various key signaling pathways. Human Tax-interacting protein 1 (TIP-1), also known as glutaminase interaction protein (GIP), is a Class I PDZ domain protein that recognizes the consensus binding motif X-S/T-X-V/I/L-COOH of the C-terminus of its target proteins. We recently reported that TIP-1 not only interacts via the C-terminus of its target partner proteins but also recognizes an internal motif defined by the consensus sequence S/T-X-V/L-D in the target protein. Identification of new target partners containing either a C-terminal or internal recognition motif has rapidly expanded the TIP-1 protein interaction network. TIP-1 being composed solely of a single PDZ domain is unique among PDZ containing proteins. Since it is involved in many important signaling pathways, it is a possible target for drug design. In this mini review, we have discussed human TIP-1, its structure, mechanism of function, its interactions with target proteins containing different recognition motifs, and its involvement in human diseases. Understanding the molecular mechanisms of TIP-1 interactions with distinct target partners and their role in human diseases will be useful for designing novel therapeutics.
Reference Key
mohanty2015biologypdz Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors ;Smita Mohanty;Mohiuddin Ovee;Monimoy Banerjee
Journal Journal of microencapsulation
Year 2015
DOI
10.3390/biology4010088
URL
http://www.mdpi.com/2079-7737/4/1/88
Keywords
structure NMR function

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