Septin 7 (SEPT7) belongs to the septin family. It forms complexes with SEPT4/SEPT8 or SEPT5/SEPT11, and appears to be a common element in most such septin complexes and it has both unusual genomic and structural features []. There are two paralogous septin 7 genes in zebrafish, sept7a and sept7b, among which Sept7b is essential for pronephric function and development of left-right asymmetry in zebrafish embryogenesis in zebrafish []. Rat SEPT7 is associated with the cytoplasmic channels of myelinating cells and is required for actin organisation in Schwann cells []. It interacts with centromere-associated protein E (CENPE) and is required for its kinetochore localisation []. C. albicans hyphae is involved in the endocytosis []. Septins were first discovered in budding yeast as a major component of bud neck filaments during cell septation [, ]. Later, its homologues were identified in nearly all eukaryotes, including humans. They are all GTP-binding proteins that are involved in diverse cellular functions, including cell cycle progression, vesicle trafficking, cytokinesis, cell migration, membrane dynamics, and chromosome segregation [, ]. Similar to cytoskeleton components such as actins and tubulins, they can assemble into filaments and bundles. However, unlike actin filaments and microtubules, septin filaments are not polar, similarly to intermediate filaments []. The number of septin genes per organism is variable: S. cerevisiae has seven and humans have 13 (SEPT1-12 and SEPT14; SEPT13 is a pseudogene now called SEPT7P2) []. All septins can form heteromeric complexes, which associate to form higher-order structures, including filaments, rings and cage-like formations [, ].
Septin 6 (SEPT6) belongs to the septin family and forms a complex with SEPT2 and SEPT7 (SEPT2/6/7) [, ]. It is required for ciliogenesis in Kupffer's vesicle, the pronephros, and the neural tube during early embryonic development in zebrafish []. Rat SEPT6 localises to microtubules in neuronal dendrite branch points and bases of protrusions [, ]. It may play a role in hepatitis C virus RNAreplication []. It forms a filamentous structure with SEPTIN12, SEPTIN2, SEPTIN7 and SEPTIN4 at the sperm annulus, required structural integrity and motility of the sperm tail during postmeiotic differentiation [].Septins were first discovered in budding yeast as a major component of bud neck filaments during cell septation [, ]. Later, its homologues were identified in nearly all eukaryotes, including humans. They are all GTP-binding proteins that are involved in diverse cellular functions, including cell cycle progression, vesicle trafficking, cytokinesis, cell migration, membrane dynamics, and chromosome segregation [, ]. Similar to cytoskeleton components such as actins and tubulins, they can assemble into filaments and bundles. However, unlike actin filaments and microtubules, septin filaments are not polar, similarly to intermediate filaments []. The number of septin genes per organism is variable: S. cerevisiae has seven and humans have 13 (SEPT1-12 and SEPT14; SEPT13 is a pseudogene now called SEPT7P2) []. All septins can form heteromeric complexes, which associate to form higher-order structures, including filaments, rings and cage-like formations [, ].
