Article citationsMore>>

Tilley, S.J., Skippen, A., Murray-Rust, J., Swigart, P.M., Stewart, A., Morgan, C.P., Cockcroft, S. and McDonald, N.Q. (2004) Structure-function analysis of phosphatidylinositol transfer protein alpha bound to human phosphatidylinositol. Structure, 12, 317-326.

has been cited by the following article:

• TITLE: Phosphatidylinositol transfer proteins: sequence motifs in structural and evolutionary analyses

  AUTHORS: Gerald J. Wyckoff, Ada Solidar, Marilyn D. Yoder

  KEYWORDS: Protein Evolution; Structural Domain; Phylogenetics; Sequence Motif

  JOURNAL NAME: Journal of Biomedical Science and Engineering, Vol.3 No.1, January 12, 2010

  ABSTRACT: Phosphatidylinositol transfer proteins (PITP) are a family of monomeric proteins that bind and transfer phosphatidylinositol and phosphatidylcholine between membrane compartments. They are required for production of inositol and diacylglycerol second messengers, and are found in most metazoan organisms. While PITPs are known to carry out crucial cell-signaling roles in many organisms, the structure, function and evolution of the majority of family members remains unexplored; primarily because the ubiquity and diversity of the family thwarts traditional methods of global alignment. To surmount this obstacle, we instead took a novel approach, using MEME and a parsimony-based analysis to create a cladogram of conserved sequence motifs in 56 PITP family proteins from 26 species. In keeping with previous functional annotations, three clades were supported within our evolutionary analysis; two classes of soluble proteins and a class of membrane-associat- ed proteins. By, focusing on conserved regions, the analysis allowed for in depth queries regarding possible functional roles of PITP proteins in both intra- and extra- cellular signaling.