CLAMP/Spef1 regulates planar cell polarity signaling and asymmetric microtubule accumulation in the <i>Xenopus</i> ciliated epithelia

Kim, Sun K.; Zhang, Siwei; Werner, Michael; Brotslaw, Eva; Mitchell, Jennifer W.; Altabbaa, Mohamed M.; Mitchell, Brian J.

doi:10.1083/jcb.201706058

Cited by 21 publications

(32 citation statements)

References 32 publications

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“…This is also represented as the arrow length (r) in figure 3g-h which is calculated as 1 - circular variance (shorter arrows = larger variance). Overall these results show that AMBMP significantly disrupts the ability of cilia to properly polarize in a manner that is consistent with what has been published for other MT regulators (Kim et al, 2018; Werner et al, 2011). …”

Section: Resultssupporting

confidence: 91%

The small molecule AMBMP disrupts microtubule growth, ciliogenesis, cell polarity, and cell migration

et al. 2018

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2-Amino-4-(3,4-(methylenedioxy)benzylamino)-6-(3-methoxyphenyl)pyrimidine (AMBMP) is a small molecule that has been previously reported to be both a Wnt agonist and a microtubule (MT) regulator. Here we report a detailed analysis of AMBMPs effects on MTs and on MT associated cellular processes including cell polarity, ciliogenesis, and cell migration. Specifically, treatment of Xenopus embryos with AMBMP leads to defects similar to the MT depolymerizing drug nocodazole, including a failure to generate or polarize cilia (depending on the timing of treatment) and a loss of the cell movements associated with radial intercalation. The dramatic effect AMBMP has on basic MT based cellular functions suggests that its usefulness as a Wnt regulator is questionable. Moreover, it may be an important new tool for experimental or pharmacological manipulation of MTs.

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Section: Resultssupporting

confidence: 91%

The small molecule AMBMP disrupts microtubule growth, ciliogenesis, cell polarity, and cell migration

et al. 2018

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“…Par3 is enriched at anteroposterior cell boundaries that are parallel to the mediolateral axis of the Xenopus neural plate, providing evidence for the polarization of a vertebrate apicobasal polarity protein in the plane of the tissue. Whereas the mechanism responsible for this planar polarization is not known, the same biochemical or mechanical signals that affect core PCP proteins ( Chien et al, 2015 ; Chu and Sokol, 2016 ) ( Kim et al, 2018 ) are likely to regulate Par3. One possibility is that the association of core PCP protein complexes with Par3 may directly contribute to Par3 enrichment at specific locations ( Banerjee et al, 2017 ; Besson et al, 2015 ).…”

Section: Discussionmentioning

confidence: 99%

Par3 interacts with Prickle3 to generate apical PCP complexes in the vertebrate neural plate

Chuykin

Ossipova

Sokol

2018

eLife

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Vertebrate neural tube formation depends on the coordinated orientation of cells in the tissue known as planar cell polarity (PCP). In the Xenopus neural plate, PCP is marked by the enrichment of the conserved proteins Prickle3 and Vangl2 at anterior cell boundaries. Here we show that the apical determinant Par3 is also planar polarized in the neuroepithelium, suggesting a role for Par3 in PCP. Consistent with this hypothesis, interference with Par3 activity inhibited asymmetric distribution of PCP junctional complexes and caused neural tube defects. Importantly, Par3 physically associated with Prickle3 and promoted its apical localization, whereas overexpression of a Prickle3-binding Par3 fragment disrupted PCP in the neural plate. We also adapted proximity biotinylation assay for use in Xenopus embryos and show that Par3 functions by enhancing the formation of the anterior apical PCP complex. These findings describe a mechanistic link between the apical localization of PCP components and morphogenetic movements underlying neurulation.

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“…CLAMP/Spef1 is a MT-associated protein which is highly expressed in ciliated epithelia, stabilizes MTs, and has been implicated in the apical accumulation of stable acetylated MTs. 165 Recently, it was shown that CLAMP/Spef1 accumulates not only at MT-rich structures, but also at junctions, and it controls planar polarity and MT asymmetry in Xenopus ciliated epithelia 166 (Figure 3). CLAMP co-localizes with components of the Par complex and interacts with aPKC, suggesting that the Par complex directs the junctional localization of CLAMP.…”

Section: Clampmentioning

confidence: 99%

The role of microtubules in the regulation of epithelial junctions

Vasileva

Citi

2018

Tissue Barriers

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The cytoskeleton is crucially important for the assembly of cell-cell junctions and the homeostatic regulation of their functions. Junctional proteins act, in turn, as anchors for cytoskeletal filaments, and as regulators of cytoskeletal dynamics and signalling proteins. The cross-talk between junctions and the cytoskeleton is critical for the morphogenesis and physiology of epithelial and other tissues, but is not completely understood. Microtubules are implicated in the delivery of junctional proteins to cell-cell contact sites, in the differentiation and spatial organization of the cytoplasm, and in the stabilization of the barrier and adhesive functions of junctions. Here we focus on the relationships between microtubules and junctions of vertebrate epithelial cells. We highlight recent discoveries on the molecular underpinnings of microtubulejunction interactions, and report new data about the interaction of cingulin and paracingulin with microtubules. We also propose a possible new role of junctions as "molecular sinks" for microtubule-associated signalling proteins.

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CLAMP/Spef1 regulates planar cell polarity signaling and asymmetric microtubule accumulation in the Xenopus ciliated epithelia

Cited by 21 publications

References 32 publications

The small molecule AMBMP disrupts microtubule growth, ciliogenesis, cell polarity, and cell migration

The small molecule AMBMP disrupts microtubule growth, ciliogenesis, cell polarity, and cell migration

Par3 interacts with Prickle3 to generate apical PCP complexes in the vertebrate neural plate

The role of microtubules in the regulation of epithelial junctions

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