Abstract
BackgroundSeptins are involved in a number of cellular processes including cytokinesis and organization of the cytoskeleton. Alterations in human septin-9 (SEPT9) levels have been linked to multiple cancers, whereas mutations in SEPT9 cause the episodic neuropathy, hereditary neuralgic amyotrophy (HNA). Despite its important function in human health, the in vivo role of SEPT9 is unknown.Methodology/Principal FindingsHere we utilize zebrafish to study the role of SEPT9 in early development. We show that zebrafish possess two genes, sept9a and sept9b that, like humans, express multiple transcripts. Knockdown or overexpression of sept9a transcripts results in specific developmental alterations including circulation defects and aberrant epidermal development.Conclusions/SignificanceOur work demonstrates that sept9 plays an important role in zebrafish development, and establishes zebrafish as a valuable model organism for the study of SEPT9.
Highlights
Septin-9 (SEPT9, MSF) is a member of the septin gene family, a conserved family of filament forming GTPases
At least 14 different septin genes have been identified in humans which, in addition to cytokinesis, play roles in vesicle trafficking, microtubule and actin function, exocytosis, establishment of cell polarity and cell motility [1,2]
Characterization of zebrafish sept9 genes Through a combination of genetic sequence analysis and BLAST searches using known human SEPT9 transcripts, we identified multiple mRNA transcripts produced from two different zebrafish sept9 genes, sept9a and sept9b. sept9a is located on chromosome 3, whereas sept9b is found on chromosome 6. sept9a produces transcripts homologous to the longest human SEPT9 isoforms 1, 2, and 3, the shortest human variant SEPT9_v7 (NCBI NM_001113496; named SEPT9_v5 in earlier literature [7]) and a unique transcript not identified in other vertebrates which we have denoted sept9a_tva
Summary
Septin-9 (SEPT9, MSF) is a member of the septin gene family, a conserved family of filament forming GTPases. At least 14 different septin genes have been identified in humans which, in addition to cytokinesis, play roles in vesicle trafficking, microtubule and actin function, exocytosis, establishment of cell polarity and cell motility [1,2]. All vertebrate septins have a highly conserved polybasic domain (PBD) followed by a GTP binding domain (GBD) homologous to those of the ras-related small GTPase family of proteins. Outside of the PBD and GBD, members of the septin family vary greatly in the length and make up of both the N- and C-termini. Despite its important function in human health, the in vivo role of SEPT9 is unknown
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