Modeling the structural implications of an alternatively spliced Exoc3l2, a paralog of the tunneling nanotube-forming M-Sec

• Published in: PloS one Vol. 13; no. 8; p. e0201557
• Main Authors: O'Callaghan, Paul, Zarb, Yvette, Noborn, Fredrik, Kreuger, Johan
• Format: Journal Article
• Language: English
• Published: United States Public Library of Science 07.08.2018; Public Library of Science (PLoS)
• Subjects: Alternative Splicing; Analysis; Animals; Biochemistry and Molecular Biology; Bioinformatics; Biokemi och molekylärbiologi; Biology and life sciences; Cell and Molecular Biology; Cell membranes; Cell- och molekylärbiologi; Deoxyribonucleic acid; DNA; Docking; exocyst complex; Gene expression; Genes; gtpase; Laboratories; Medical Cell Biology; Medicine and Health Sciences; Medicinsk cellbiologi; Membrane vesicles; Messenger RNA; Mice; migration; Models, Molecular; Molecular biology; mRNA; Nanotubes; Protein Conformation; Proteins; rala; Research and Analysis Methods; RNA - metabolism; Secretory vesicles; Sequence Analysis, RNA; SNAP receptors; Structure; subunit; Tumor Necrosis Factors - chemistry; Tumor Necrosis Factors - genetics; Tunneling; Vesicular Transport Proteins - chemistry; Vesicular Transport Proteins - genetics; United States > US; Sweden
• ISSN: 1932-6203; 1932-6203
• DOI: 10.1371/journal.pone.0201557

The exocyst is a molecular tether that retains secretory vesicles at the plasma membrane prior to SNARE-mediated docking and fusion. However, individual exocyst complex components (EXOCs) may also function independently of exocyst assembly. Alternative splice variants of EXOC mRNA and paralogs of EXOC genes have been described and several have been attributed functions that may be independent of the exocyst complex. Here we describe a novel splice variant of murine Exoc3l2, which we term Exoc3l2a. We discuss possible functional implications of the resulting domain excision from this isoform of EXOC3L2 based on structural similarities with its paralog M-Sec (EXOC3L3), which is implicated in tunneling nanotube formation. The identification of this Exoc3l2 splice variant expands the potential for subunit diversity within the exocyst and for alternative functionality of this component independently of the exocyst.