Septins 2, 7 and 9 and MAP4 colocalize along the axoneme in the primary cilium and control ciliary length

Ghossoub, Rania; Hu, Qiao‐Sheng; Failler, Marion; Rouyez, M C; Spitzbarth, Benjamin; Mostowy, Serge; Wolfrum, Uwe; Saunier, Sophie; Cossart, Pascale; Nelson, W. James; Benmerah, Alexandre

doi:10.1242/dev.100073

Cited by 29 publications

(62 citation statements)

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“…In the ciliated cells in the zebrafish, septin 7 is localized to the epithelium, at the base of the cilium and along the ciliary axoneme, depending on the tissue analyzed. This kind of wide expression and variation of localization that is dependent on the cell type corresponds to the previously published localization of septin 7 in cultured cells and Xenopus embryos (Ghossoub et al, 2013;Kim et al, 2010). In cultured retinal pigmented epithelial cells, septin 7 localizes to the cytoplasm and a small proportion of the protein is found along extended mature primary cilia (Ghossoub et al, 2013).…”

Section: Discussionsupporting

confidence: 85%

“…The distribution of septin 7 in the cytoplasm of ciliated cells in zebrafish suggests that septin 7 could have roles that are additional to its function as a ciliary membrane diffusion barrier (Chih et al, 2011;Hu et al, 2010) or a possible component of the ciliary axoneme (Ghossoub et al, 2013). As septins are known to function in vesicle trafficking (Beites et al, 1999;Hsu et al, 1998;Wasik et al, 2012), we hypothesized that septin 7 could be involved in the trafficking processes associated with ciliogenesis.…”

Section: Septin 7 Physically Interacts With Rab8mentioning

confidence: 99%

“…Septin 2, 6 and 7 have been reconstituted into filaments, and the filament structure has been solved by X-ray crystallography (Sirajuddin et al, 2007). Septin 2 and 7 localize at the base of the primary cilium of epithelial cells in tissue culture and Xenopus epidermis, and expression of the complex is required for ciliogenesis (Ghossoub et al, 2013;Hu et al, 2010;Kim et al, 2010) and as a ciliary membrane protein diffusion barrier (Chih et al, 2011;Hu et al, 2010). Septin 7 is expressed in glomerular epithelial cells (podocytes) in mouse and rat, and regulates glucose transporter trafficking in cultured podocytes (Wasik et al, 2012).…”

Section: Introductionmentioning

confidence: 99%

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Sept7bis essential for pronephric function and development of left-right asymmetry in zebrafish embryogenesis

Dash

Lehtonen

Wasik

et al. 2014

Journal of Cell Science

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The conserved septin family of filamentous small GTPases plays important roles in mitosis, cell migration and cell morphogenesis by forming scaffolds and diffusion barriers. Recent studies in cultured cells in vitro indicate that a septin complex of septin 2, 7 and 9 is required for ciliogenesis and cilia function, but septin function in ciliogenesis in vertebrate organs in vivo is not understood. We show that sept7b is expressed in ciliated cells in different tissues during early zebrafish development. Knockdown of sept7b by using morpholino antisense oligonucleotides caused misorientation of basal bodies and cilia, reduction of apical actin and the shortening of motile cilia in Kupffer's vesicle and pronephric tubules. This resulted in pericardial and yolk sac edema, body axis curvature and hydrocephaly. Notably, in sept7b morphants we detected strong leftright asymmetry defects in the heart and lateral plate mesoderm (situs inversus), reduced fluid flow in the kidney, the formation of kidney cysts and loss of glomerular filtration barrier function. Thus, sept7b is essential during zebrafish development for pronephric function and ciliogenesis, and loss of expression of sept7b results in defects that resemble human ciliopathies.

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Section: Discussionsupporting

confidence: 85%

Section: Septin 7 Physically Interacts With Rab8mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Sept7bis essential for pronephric function and development of left-right asymmetry in zebrafish embryogenesis

Dash

Lehtonen

Wasik

et al. 2014

Journal of Cell Science

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“…• septin workshop confirmed a role for SEPT9 in controlling cilia length (Ghossoub et al, 2013), and showed that a novel signalling pathway downstream of SEPT9 enables the growth of axonemal microtubules by stabilizing microtubule plus ends. The diversity of septin localizations and functions is reviewed by Dolat and colleagues, who provide a comprehensive account of septin functions in tissue and organ systems, and discuss how abnormal septin expression leads to the pathogenesis of tissue-specific diseases (Dolat et al, 2014; …”

mentioning

confidence: 85%

Highlight: The 5th International Workshop on Septin Biology

Mostowy

Füchtbauer

et al. 2013

Biological Chemistry

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“…Septins interact with actin through proteins like anillin, which recruits septins to the actomyosin ring during cell division, non-muscle myosin II during interphase, a septin associated RhoGEF, and the Rho effector rhotekin [46,[51][52][53]. Septin association with microtubules is less well understood, with the microtuble-associated protein, MAP4, as the only known protein known to bridge this interaction [38,54]. H2AX on serine 139 (!H2AX), which promotes recruitment of other DDR proteins including chromatin modifying complexes [98,99].…”

Section: Gdp (B) Surface Representation Of the Sept2-sept6-sept7 Commentioning

confidence: 99%

Novel Pathways Linking Mammalian Septins and the DNA Damage Response

Errington¹

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A cellular response to damaged DNA, known as the DNA damage response (DDR), has evolved to combat damage that occurs from exposure to genotoxic agents or byproducts of normal cellular metabolism. Upon recognition of DNA damage, the cell arrests the cell cycle and repairs damaged DNA to maintain genome integrity. However, if the damage is severe, cells undergo apoptosis or initiate cellular senescence. The DDR is a highly coordinated event linking many pathways involved in various cellular processes. A previous study from this lab implicated mammalian septins in the DDR, although through an unknown mechanism. These cytoskeletal proteins function as signaling platforms and diffusion barriers and associate with various proteins including the adaptor proteins SOCS7 and NCK. In response to multiple types of DNA damage, NCK relocalizes from the cytoplasm to the nucleus, using the nucleocytoplasmic shuttling protein SOCS7. The nuclear accumulation of NCK in response to UV irradiation is dependent on the kinase activity of ATR, a member of the PIKK family that is activated early in the DDR. Depletion of NCK results in elevated phosphorylation of the transcription factor p53 and an early induction of apoptosis. Depletion of SOCS7, which blocks the nuclear accumulation of NCK, also increases phosphorylation of p53 and also results in an early induction of apoptosis. This indicates the anti-apoptotic role of NCK is dependent on its nuclear translocation during the DDR. Another septin interacting protein was identified using a proteomic approach. This novel nuclease called Taken together, these data demonstrate that mammalian septins play a role in the DDR and highlight an unexpected link between cytoskeletal elements and DNA damage signaling.

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Septins 2, 7 and 9 and MAP4 colocalize along the axoneme in the primary cilium and control ciliary length

Cited by 29 publications

References 1 publication

Sept7bis essential for pronephric function and development of left-right asymmetry in zebrafish embryogenesis

Sept7bis essential for pronephric function and development of left-right asymmetry in zebrafish embryogenesis

Highlight: The 5th International Workshop on Septin Biology

Novel Pathways Linking Mammalian Septins and the DNA Damage Response

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