F-actin binding protein, anillin, regulates integrity of intercellular junctions in human epithelial cells

Wang, Dongdong; Chadha, Gibran; Feygin, Alex; Ivanov, Andrei I.

doi:10.1007/s00018-015-1890-6

Cited by 44 publications

(43 citation statements)

References 86 publications

(107 reference statements)

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“…Scinderin is an important regulator of F-actin organisation, and F-actin is important in regulating the integrity of intercellular junctions in human epithelial cells, as reported by previous studies [4,15]. In our study, we demonstrated that loss of SCIN decreased the EGFR protein level significantly.…”

Section: Discussionsupporting

confidence: 86%

Loss of scinderin decreased expression of epidermal growth factor receptor and promoted apoptosis of castration‐resistant prostate cancer cells

Lai

Zhao³

et al. 2018

FEBS Open Bio

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Most patients with prostate cancer will eventually develop the castration‐resistant form characterised by metastasis. Cytoskeleton constituents, including F‐actin, play important roles in maintaining epithelial integrity and their disruption is a major cause of cancer progression. We previously showed that scinderin (SCIN), an important regulator of F‐actin organisation, is highly expressed in poorly differentiated cancer tissues. This study aimed to explore the mechanism of its regulation of cell proliferation. We discovered that SCIN knockdown significantly downregulated epidermal growth factor receptor (EGFR) protein expression, and inhibited epidermal growth factor (EGF)‐mediated cell proliferation and activation of the downstream mitogen‐activated protein kinase kinase (MEK)/extracellular signal‐regulated kinase (ERK) signalling pathway. Silencing of SCIN promoted apoptosis in two cell lines (PC‐3 and DU145), inhibited B‐cell lymphoma‐extra‐large (Bcl‐xl) expression and activated caspase signalling. Furthermore, in vivo studies showed that SCIN deletion slowed tumour growth and decreased EGFR expression. Thus, we conclude that SCIN promotes prostate cancer cell survival by stabilising EGFR and MEK/ERK signalling.

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Section: Discussionsupporting

confidence: 86%

Loss of scinderin decreased expression of epidermal growth factor receptor and promoted apoptosis of castration‐resistant prostate cancer cells

Lai

Zhao³

et al. 2018

FEBS Open Bio

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“…In mammalian epithelial cells (DU145 and SK-CO15), depletion of Anillin disrupted junctions despite the fact that Anillin localization could not be detected at junctions. Instead, loss of Anillin misregulated junctions through the JNK pathway (Wang et al, 2015) (Figure 4C). …”

Section: Scaffold Proteins Regulate Rho Gtpase Output At Cell-cell Jumentioning

confidence: 99%

Rho GTPases and actomyosin: Partners in regulating epithelial cell-cell junction structure and function

Arnold

Stephenson

Miller

2017

Experimental Cell Research

122

118

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Epithelial tissues are defined by polarized epithelial cells that are integrated into tissues and exhibit barrier function in order to regulate what is allowed to pass between cells. Cell-cell junctions must be stable enough to promote barrier function and tissue integrity, yet plastic enough to remodel when necessary. This remarkable ability to dynamically sense and respond to changes in cell shape and tissue tension allows cell-cell junctions to remain functional during events that disrupt epithelial homeostasis including morphogenesis, wound healing, and cell division. In order to achieve this plasticity, both tight junctions and adherens junctions are coupled to the underlying actomyosin cytoskeleton. Here, we discuss the importance of the junctional linkage to actomyosin and how a localized zone of active RhoA along with other Rho GTPases work together to orchestrate junctional actomyosin dynamics. We focus on how scaffold proteins help coordinate Rho GTPases, their upstream regulators, and their downstream effectors for efficient, localized Rho GTPase signaling output. Additionally, we highlight important roles junctional actin-binding proteins play in addition to their traditional roles in organizing actin. Together, Rho GTPases, their regulators, and effectors form compartmentalized signaling modules that regulate actomyosin structure and contractility to achieve proper cell-cell adhesion and tissue barriers.

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“…Therefore mechanisms by which C3 toxin and Anillin siRNA interfere with RhoA are distinct. It was shown that Myosin II activity was not involved in the regulation of intercellular junctions by Anilin in human epithelial (Wang et al, 2015) and we found in osteoclasts that Anillin siRNA does not affect Myosin II activity.…”

Section: Discussionmentioning

confidence: 45%

“…Anillin silencing was also found to increased Jun kinase (JNK) activity in epithelial cells (Wang et al, 2015). JNK is essential downstream of RANK for osteoclast differentiation (Touaitahuata et al, 2014) and also for the formation of podosome rosettes in SrcY527Ftransformed NIH3T3 fibroblasts (Pan et al, 2013), but whether JNK controls osteoclast actin cytoskeleton organization and resorption activity is unknown to date.…”

Section: Discussionmentioning

confidence: 99%

Combined strategy of siRNA and osteoclast actin cytoskeleton automated imaging to identify novel regulators of bone resorption shows a non-mitotic function for anillin

Maurin¹,

Morel²,

Hassen‐Khodja

et al. 2018

Preprint

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Osteoclasts are the main cells responsible for the resorption of mineralized extracellular matrices. They are the major targets for anti-resorptive therapies to manage osteoporosis, a major public health problem. Osteoclasts are giant multinucleated cells that can organize their a unique adhesion structure based on a belt of podosomes, which is the keystone of the bone resorption apparatus. We combined differential transcriptomics and siRNA screening approaches to get a broader view of cytoskeletal regulators that participate in the control of osteoclast cytoskeleton and identify novel regulators of bone resorption by osteoclasts. We identified 20 new candidate regulators of osteoclasts cytoskeleton including Fkbp15, Spire1, Tacc2 and RalA, for which we confirmed they are necessary for proper organization of the podosome belt. We also showed that Anillin, well known for its role during cytokinesis, is essential in osteoclasts for correct podosome patterning and efficient bone resorption. In particular, Anillin controls the levels of the GTPase RhoA, a known regulator of osteoclast cytoskeleton and resorption activity. Finally, we set up and validated an automated imaging strategy based on open-source software for automatic and objective measurement of actin cytoskeleton organization in osteoclasts. We provide these pipelines that are useful to automatically assess the effect of collections of siRNAs or chemical compounds on osteoclast cytoskeleton or differentiation. 4Introduction.

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F-actin binding protein, anillin, regulates integrity of intercellular junctions in human epithelial cells

Cited by 44 publications

References 86 publications

Loss of scinderin decreased expression of epidermal growth factor receptor and promoted apoptosis of castration‐resistant prostate cancer cells

Loss of scinderin decreased expression of epidermal growth factor receptor and promoted apoptosis of castration‐resistant prostate cancer cells

Rho GTPases and actomyosin: Partners in regulating epithelial cell-cell junction structure and function

Combined strategy of siRNA and osteoclast actin cytoskeleton automated imaging to identify novel regulators of bone resorption shows a non-mitotic function for anillin

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