ROCK-mediated contractility, tight junctions and channels contribute to the conversion of a preapical patch into apical surface during isochoric lumen initiation

Ferrari, Aldo; Veligodskiy, Alexey; Berge, Ulrich; Lucas, Miriam S.; Kroschewski, Ruth

doi:10.1242/jcs.018648

Cited by 112 publications

(140 citation statements)

References 65 publications

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“…From 120 minutes to 240 minutes, the lumen volume increased 1.4 times to 8000 μm 3 . In this second phase, our rate of increase is comparable to that seen by Ferrari et al (2008). Although we did not fit such early data points, our model reproduces results comparable to the measurements of Ferrari et al (2008).…”

supporting

confidence: 61%

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A model for cyst lumen expansion and size regulation via fluid secretion

Gin

Tanaka

Brusch

2010

Journal of Theoretical Biology

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supporting

confidence: 61%

“…Ferrari et al (2008) also measured cyst lumen volumes, focusing on earlier time points. They investigated the development of single MDCK cells into aggregates and found that initially, the lumen volume increases without changes in the total volume or cell number.…”

mentioning

confidence: 99%

A model for cyst lumen expansion and size regulation via fluid secretion

Gin

Tanaka

Brusch

2010

Journal of Theoretical Biology

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“…However, it suggests that Grhl2-deficient collecting duct cells exhibit a defect of lumen expansion that occurs subsequent to adequate cell alignment and polarization. Because previous studies indicated that lumen expansion is driven by fluid accumulation [34][35][36][37] and requires the formation of tight paracellular barriers, 36 we propose that GRHL2 regulates lumen expansion by stabilizing the epithelial barrier via CLDN4 and facilitating apical fluid excretion via RAB25. However, this hypothesis will require additional experimental support.…”

Section: Discussionmentioning

confidence: 87%

A Grainyhead-Like 2/Ovo-Like 2 Pathway Regulates Renal Epithelial Barrier Function and Lumen Expansion

Aue

Hinze

Walentin

et al. 2015

Journal of the American Society of Nephrology

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Grainyhead transcription factors control epithelial barriers, tissue morphogenesis, and differentiation, but their role in the kidney is poorly understood. Here, we report that nephric duct, ureteric bud, and collecting duct epithelia express high levels of grainyhead-like homolog 2 (Grhl2) and that nephric duct lumen expansion is defective in Grhl2-deficient mice. In collecting duct epithelial cells, Grhl2 inactivation impaired epithelial barrier formation and inhibited lumen expansion. Molecular analyses showed that GRHL2 acts as a transcriptional activator and strongly associates with histone H3 lysine 4 trimethylation. Integrating genome-wide GRHL2 binding as well as H3 lysine 4 trimethylation chromatin immunoprecipitation sequencing and gene expression data allowed us to derive a high-confidence GRHL2 target set. GRHL2 transactivated a group of genes including Ovol2, encoding the ovo-like 2 zinc finger transcription factor, as well as E-cadherin, claudin 4 (Cldn4), and the small GTPase Rab25. Ovol2 induction alone was sufficient to bypass the requirement of Grhl2 for E-cadherin, Cldn4, and Rab25 expression. Re-expression of either Ovol2 or a combination of Cldn4 and Rab25 was sufficient to rescue lumen expansion and barrier formation in Grhl2-deficient collecting duct cells. Hence, we identified a Grhl2/Ovol2 network controlling Cldn4 and Rab25 expression that facilitates lumen expansion and barrier formation in subtypes of renal epithelia. The renal collecting duct's vital electrolyte and waterregulatory functions are carried out by highly specialized cell populations. 1 The collecting duct itself is composed of a tight epithelium, which separates the urinary compartment from a hypertonic interstitium and maintains a barrier to concentration gradients. The collecting duct derives from the ureteric bud, which emanates from the nephric duct and then undergoes branching morphogenesis in response to signals from the adjacent metanephric mesenchyme. 2 Many of the genes that are critical for aspects of nephric duct development continue to be expressed in the ureteric bud and collecting duct, serving roles in development, differentiation, and maintenance of these cells (e.g., Pax2/8, Gata3, Emx2, and Hnf1b). 3 Little is known about the molecular pathways governing the specific epithelial properties of these cells, although it is clear that these epithelia share several cell biologic properties such as a uniform tubular appearance characterized by a cuboidal epithelium surrounding a fluid-filled lumen and a molecular composition of the apical junctional complex that includes

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“…De novo generation of the apical lumen requires Rab8a-and Rab11a-dependent transport of the apical membrane resident protein podocalyxin/gp135 (PCX; ref. 19) to regions between neighboring cells to initiate lumen formation (10,20).…”

Section: Mutations In Myo5b Independently Affect Localization Of Eithermentioning

confidence: 99%

“…The mCherry-Myo5BΔD overlapped with PCX at the preapical patch (ref. 20; Fig. 3Bb), a luminal domain precursor consisting of a nonexpanded luminal space with closely opposed membranes, but devoid of cell-cell junctions (β-catenin; Fig.…”

Section: Mutations In Myo5b Independently Affect Localization Of Eithermentioning

confidence: 99%

Rab GTPase–Myo5B complexes control membrane recycling and epithelial polarization

Roland

Bryant

Datta

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

181

201

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The Rab GTPases are the largest family of proteins regulating membrane traffic. Rab proteins form a nidus for the assembly of multiprotein complexes on distinct vesicle membranes to regulate particular membrane trafficking pathways. Recent investigations have demonstrated that Myosin Vb (Myo5B) is an effector for Rab8a, Rab10, and Rab11a, all of which are implicated in regulating different pathways for recycling of proteins to the plasma membrane. It remains unclear how specific interactions of Myo5B with individual Rab proteins can lead to specificity in the regulation of alternate trafficking pathways. We examined the relative contributions of Rab/Myo5B interactions with specific pathways using Myo5B mutants lacking binding to either Rab11a or Rab8a. Myo5B Q1300L and Y1307C mutations abolished Rab8a association, whereas Myo5B Y1714E and Q1748R mutations uncoupled association with Rab11a. Expression of Myo5B tails containing these mutants demonstrated that Rab11a, but not Rab8a, was required for recycling of transferrin in nonpolarized cells. In contrast, in polarized epithelial cyst cultures, Myo5B was required for apical membrane trafficking and de novo lumen formation, dependent on association with both Rab8a and Rab11a. These data demonstrate that different combinations of Rab GTPase association with Myo5B control distinct membrane trafficking pathways.

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ROCK-mediated contractility, tight junctions and channels contribute to the conversion of a preapical patch into apical surface during isochoric lumen initiation

Abstract: SummaryROCK-mediated contractility, tight junctions and channels contribute to the conversion of a preapical patch into apical surface during isochoric lumen initiation

Cited by 112 publications

References 65 publications

A model for cyst lumen expansion and size regulation via fluid secretion

A model for cyst lumen expansion and size regulation via fluid secretion

A Grainyhead-Like 2/Ovo-Like 2 Pathway Regulates Renal Epithelial Barrier Function and Lumen Expansion

Rab GTPase–Myo5B complexes control membrane recycling and epithelial polarization

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