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SEPT7 encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae.
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study identified control of septin (show SEPT6 Proteins) localization by the planar cell polarity (PCP (show PRCP Proteins)) protein Fritz (show WDPCP Proteins) as a crucial control point for both collective cell movement and ciliogenesis in embryos
Study discloses both SEPT2 (show SEPT2 Proteins) and SEPT7 are essential for breast cancer cell migration and invasion by controlling MEK (show MAP2K1 Proteins)/ERK (show EPHB2 Proteins) MAPKs activation.
SUMOylation of human septins is critical for septin (show SEPT6 Proteins) filament bundling and cytokinesis.
Low SEPT7 expression is associated with glioma cell invasion.
Results show that SEPT7 is involved in glioma cell migration with the assistance of cofilin (show CFL1 Proteins) phosphomediated cytoskeleton locomotion.
Septin6 and Septin7 GTP binding proteins regulate AP-3- and ESCRT-dependent multivesicular body biogenesis
Significantly lower SEPT7 expression in encapsulated follicular variant of papillary thyroid carcinoma may be a sign of different molecular signature in this type of tissue.
In response to Candida albicans infection, SEPT7 forms a complex with endothelial cell N-cadherin (show CDH2 Proteins), is required for normal accumulation of N-cadherin (show CDH2 Proteins) around hyphae, and is necessary for maximal fungal endocytosis.
SEPT2 (show SEPT2 Proteins) forms a 1:1:1 complex with SEPT7 and SEPT9 (show SEPT9 Proteins).
Overexpression of the yeast septin7 ortholog CDC10 also conferred resistance to the negative effects of copper as well as protecting cells from the overexpression of Bax (show BAX Proteins).
miR (show MLXIP Proteins)-30a-5p is a bona fide negative regulator of SEPT7 and the oncogenic activity of miR (show MLXIP Proteins)-30a-5p in human gliomas is at least in part through the repression of SEPT7
These findings point to a possible pathogenetic role of septin 7 in Equine recurrent uveitis.
a SNP in the CDC10 gene was associated with growth-related traits in Japanese Black beef cattle
SEPT7 regulates gross morphogenesis of the inner ear and maintains the size of the inner ear sensory epithelial area. It does not affect differentiation of hair cells and supporting cells. It exerts its effects at an early developmental stage of the inner ear.
Sept7-deficient T cells failed to complete cytokinesis when prompted by pharmacological activation or cytokines. In contrast, cell division was not dependent on sept7 when cell-cell contacts, such as those with antigen-presenting cells, provided a niche.
We identified stathmin (show STMN1 Proteins) as a key molecule aiding in septin (show SEPT6 Proteins)-independent cytokinesis, demonstrated that stathmin (show STMN1 Proteins) supplementation is sufficient to override cytokinesis failure in SEPT7-null fibroblasts
Sept7 provides a physical scaffold for HDAC6 (show HDAC6 Proteins) to achieve efficient microtubule deacetylation, thereby negatively regulating microtubule stability to an optimal level for neuritogenesis.
Septin 7 may regulate meiotic cell cycle progression by affecting microtubule cytoskeletal dynamics in mouse oocytes.
Report SEPT4 (show SEPT4 Proteins)/5/7 expression in mouse cochlea and roles in auditory function.
performed large-scale interaction screens to understand the neuronal functions of the ERK3 (show RYK Proteins)/MK5 (show MAPKAPK5 Proteins) pathway and identified septin7 (Sept7) as a novel interacting partner of ERK3 (show RYK Proteins)
In Sept9 (show SEPT9 Proteins) knockout cells, long septin (show SEPT6 Proteins) filaments stained for Sept7 disappeared. Instead, staining was found in short, often curved filaments and rings. Furthermore, Sept7 was no longer localized to the mitotic spindle
SEPT7 is involved in the regulation of subcellular-compartment formation during spermiogenesis in the mouse.
This gene encodes a protein that is highly similar to the CDC10 protein of Saccharomyces cerevisiae. The protein also shares similarity with Diff 6 of Drosophila and with H5 of mouse. Each of these similar proteins, including the yeast CDC10, contains a GTP-binding motif. The yeast CDC10 protein is a structural component of the 10 nm filament which lies inside the cytoplasmic membrane and is essential for cytokinesis. This human protein functions in gliomagenesis and in the suppression of glioma cell growth, and it is required for the association of centromere-associated protein E with the kinetochore. Alternative splicing results in multiple transcript variants. Several related pseudogenes have been identified on chromosomes 5, 7, 9, 10, 11, 14, 17 and 19.
, septin 7
, cell division cycle 10
, CDC10 protein homolog
, CDC10 cell division cycle 10-like
, CDC10 (cell division cycle 10, S. cerevisiae, homolog)
, cell division cycle 10 homolog
, CDC10 (cell division cycle 10, S.cerevisiae, homolog)