Alternative Splicing as a Mechanism for Regulating 14-3-3 Binding: Interactions between hD53 (TPD52L1) and 14-3-3 Proteins

• Published in: Journal of molecular biology Vol. 332; no. 3; pp. 675 - 687
• Main Authors: Boutros, Rose, Bailey, Angela M, Wilson, Sarah H.D, Byrne, Jennifer A
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 19.09.2003
• Subjects: 14-3-3; 14-3-3 Proteins; Alternative Splicing; Binding Sites; Breast Neoplasms - metabolism; Carcinoma - metabolism; Cytoplasm - metabolism; Exons; Female; gene structure; Humans; Immune Sera; Neoplasm Proteins - genetics; Neoplasm Proteins - immunology; Neoplasm Proteins - metabolism; Precipitin Tests; Protein Binding - physiology; protein–protein interactions; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Solubility; TPD52; Tumor Cells, Cultured; Two-Hybrid System Techniques; Tyrosine 3-Monooxygenase - genetics; Tyrosine 3-Monooxygenase - metabolism; TPD52; 14-3-3; gene structure; protein–protein interactions; PBS; RT; alternative splicing; ins3; TBS; Th; Y2H

D52 (TPD52)-like proteins are coiled-coil motif-bearing proteins first identified through their expression in human breast carcinoma, which have been proposed to represent signalling intermediates and regulators of vesicle trafficking. D52-like gene transcripts are subject to alternative splicing, w...