Apico-basal elongation requires a drebrin-E–EB3 complex in columnar human epithelial cells

Bazellières, Elsa; Massey-Harroche, Dominique; Barthélémy-Requin, Magali; Richard, Fabrice; Arsanto, Jean-Pierre; Bivic, André Le

doi:10.1242/jcs.092676

Cited by 36 publications

(42 citation statements)

References 46 publications

(38 reference statements)

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“…The enrichment of protein catabolic pathways is consistent with smoke-exposure studies in alveolar cells that have demonstrated increased endoplasmic reticulum stress and protein degradation [20]. The role of actin and cytoskeletal processes in response to smoking is less well understood, but cytoskeletal-associated pathways containing genes such as ACTN1 and DBN1 have been associated with roles in immune cell activation [21] and columnar epithelial cell function [22]. These data point to further avenues for investigation of the specific nature of inflammatory, catabolic, and cytoskeletal responses in circulating immune cells in smokers.…”

Section: Discussionsupporting

confidence: 59%

COPD subtypes identified by network-based clustering of blood gene expression

et al. 2016

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One of the most common smoking-related diseases, chronic obstructive pulmonary disease (COPD), results from a dysregulated, multi-tissue inflammatory response to cigarette smoke. We hypothesized that systemic inflammatory signals in genome-wide blood gene expression can identify clinically important COPD-related disease subtypes, and we leveraged pre-existing gene interaction networks to guide unsupervised clustering of blood microarray expression data. Using network-informed non-negative matrix factorization, we analyzed genome-wide blood gene expression from 229 former smokers in the ECLIPSE Study, and we identified novel, clinically relevant molecular subtypes of COPD. These network-informed clusters were more stable and more strongly associated with measures of lung structure and function than clusters derived from a network-naïve approach, and they were associated with subtype-specific enrichment for inflammatory and protein catabolic pathways. These clusters were successfully reproduced in an independent sample of 135 smokers from the COPDGene Study.

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Section: Discussionsupporting

confidence: 59%

COPD subtypes identified by network-based clustering of blood gene expression

et al. 2016

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“…Knockdown of c-Yes by ϳ75% did not affect the expression of several actin regulatory proteins, including 1) Arp3 and N-WASP, which are known to induce branched actin polymerization (11,22,49), 2) actin-binding protein drebrin E, which is known to recruit Arp3 to the BTB to elicit its restructuring at stage VIII of the epithelial cycle (4,34), and 3) Eps8, an actin barbed-end capping and bundling protein in the testis ( Fig. 2A) (2,37).…”

Section: Knockdown Of C-yes In Sertoli Cells By Rnai Accelerates Actimentioning

confidence: 97%

c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution

Xiao

Mruk

Cheng

2013

American Journal of Physiology-Endocrinology and Metabolism

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During spermatogenesis, extensive restructuring takes place at the cell-cell interface since developing germ cells migrate progressively from the basal to the adluminal compartment of the seminiferous epithelium. Since germ cells per se are not motile cells, their movement relies almost exclusively on the Sertoli cell. Nonetheless, extensive exchanges in signaling take place between these cells in the seminiferous epithelium. c-Yes, a nonreceptor protein tyrosine kinase belonging to the Src family kinases (SFKs) and a crucial signaling protein, was recently shown to be upregulated at the Sertoli cell-cell interface at the blood-testis barrier (BTB) at stages VIII-IX of the seminiferous epithelial cycle of spermatogenesis. It was also highly expressed at the Sertoli cell-spermatid interface known as apical ectoplasmic specialization (apical ES) at stage V to early stage VIII of the epithelial cycle during spermiogenesis. Herein, it was shown that the knockdown of c-Yes by RNAi in vitro and in vivo affected both Sertoli cell adhesion at the BTB and spermatid adhesion at the apical ES, causing a disruption of the Sertoli cell tight junction-permeability barrier function, germ cell loss from the seminiferous epithelium, and also a loss of spermatid polarity. These effects were shown to be mediated by changes in distribution and/or localization of adhesion proteins at the BTB (e.g., occludin, N-cadherin) and at the apical ES (e.g., nectin-3) and possibly the result of changes in the underlying actin filaments at the BTB and the apical ES. These findings implicate that c-Yes is a likely target of male contraceptive research.testis; c-Yes; nonreceptor protein tyrosine kinase; Sertoli cell; spermatogenesis; seminiferous epithelial cycle; ectoplasmic specialization DURING SPERMATOGENESIS, EXTENSIVE RESTRUCTURING and communication take place at the Sertoli cell-cell and Sertoli-germ cell interface across the seminiferous epithelium to accommodate germ cell movement and to coordinate cellular events that occur simultaneously at different stages of the seminiferous epithelial cycle in the mammalian testis (12,23,48). For instance, at stage VIII of the epithelial cycle, preleptotene spermatocytes, differentiated from type B spermatogonia, residing in the basal compartment traverse the blood-testis barrier (BTB) to enter the adluminal compartment while transforming to leptotene and zygote spermatocytes to prepare for meiosis I/II (23, 48). However, fully developed spermatids that become spermatozoa at the adluminal edge of the tubule lumen undergo spermiation; the release of sperm also takes place at stage VIII of the cycle, involving degeneration of the apical ectoplasmic specialization (apical ES) at the Sertoli-spermatid

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“…Drebrin is a neuronally expressed actin filament binding protein that has been involved in the regulation of neuronal morphology (Dun and Chilton, 2010; Dun et al, 2012). Drebrin can bundle actin filaments (Worth et al, 2013), regulate the binding of additional actin binding proteins to filaments (reviewed in Dun and Chilton, 2010) and importantly can also directly associate with microtubule plus tips through the end binding (EB) proteins (Geraldo et al, 2008; Bazellières et al, 2012). While there are multiple possible molecules involved in branching that have the potential to bind actin filaments and microtubules and thus serve as coordinators between these two cytoskeletal systems, no study to date has simultaneously addressed the role of any of these molecules in the regulation of the both the actin and microtubule cytoskeleton during branching.…”

Section: Introductionmentioning

confidence: 99%

Drebrin coordinates the actin and microtubule cytoskeleton during the initiation of axon collateral branches

Ketschek

Spillane

Dun

et al. 2016

Developmental Neurobiology

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Drebrin is a cytoskeleton-associated protein which can interact with both actin filaments and the tips of microtubules. Its roles have been studied mostly in dendrites, and the functions of drebrin in axons are less well understood. In this work we analyzed the role of drebrin, through shRNA-mediated depletion and over-expression, in the collateral branching of chicken embryonic sensory axons. We report that drebrin promotes the formation of axonal filopodia and collateral branches in vivo and in vitro. Live imaging of cytoskeletal dynamics revealed that drebrin promotes the formation of filopodia from precursor structures termed axonal actin patches. Endogenous drebrin localizes to actin patches and depletion studies indicate that drebrin contributes to the development of patches. In filopodia, endogenous drebrin localizes to the proximal portion of the filopodium. Drebrin was found to promote the stability of axonal filopodia and the entry of microtubule plus tips into axonal filopodia. The effects of drebrin on the stabilization of filopodia are independent of its effects on promoting microtubule targeting to filopodia. Inhibition of myosin II induces a redistribution of endogenous drebrin distally into filopodia, and further increases branching in drebrin overexpressing neurons. Finally, a 30 minute treatment with the branch inducing signal nerve growth factor increases the levels of axonal drebrin. The current study determines the specific roles of drebrin in the regulation of the axonal cytoskeleton, and provides evidence that drebrin contributes to the coordination of the actin and microtubule cytoskeleton during the initial stages of axon branching.

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Apico-basal elongation requires a drebrin-E–EB3 complex in columnar human epithelial cells

Cited by 36 publications

References 46 publications

COPD subtypes identified by network-based clustering of blood gene expression

COPD subtypes identified by network-based clustering of blood gene expression

c-Yes regulates cell adhesion at the apical ectoplasmic specialization-blood-testis barrier axis via its effects on protein recruitment and distribution

Drebrin coordinates the actin and microtubule cytoskeleton during the initiation of axon collateral branches

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