@article{14826,
  abstract     = {The plant-signaling molecule auxin triggers fast and slow cellular responses across land plants and algae. The nuclear auxin pathway mediates gene expression and controls growth and development in land plants, but this pathway is absent from algal sister groups. Several components of rapid responses have been identified in Arabidopsis, but it is unknown if these are part of a conserved mechanism. We recently identified a fast, proteome-wide phosphorylation response to auxin. Here, we show that this response occurs across 5 land plant and algal species and converges on a core group of shared targets. We found conserved rapid physiological responses to auxin in the same species and identified rapidly accelerated fibrosarcoma (RAF)-like protein kinases as central mediators of auxin-triggered phosphorylation across species. Genetic analysis connects this kinase to both auxin-triggered protein phosphorylation and rapid cellular response, thus identifying an ancient mechanism for fast auxin responses in the green lineage.},
  author       = {Kuhn, Andre and Roosjen, Mark and Mutte, Sumanth and Dubey, Shiv Mani and Carrillo Carrasco, Vanessa Polet and Boeren, Sjef and Monzer, Aline and Koehorst, Jasper and Kohchi, Takayuki and Nishihama, Ryuichi and Fendrych, Matyas and Sprakel, Joris and Friml, Jiří and Weijers, Dolf},
  issn         = {1097-4172},
  journal      = {Cell},
  keywords     = {General Biochemistry, Genetics and Molecular Biology},
  number       = {1},
  pages        = {130--148.e17},
  publisher    = {Elsevier},
  title        = {{RAF-like protein kinases mediate a deeply conserved, rapid auxin response}},
  doi          = {10.1016/j.cell.2023.11.021},
  volume       = {187},
  year         = {2024},
}

@article{10573,
  abstract     = {How tissues acquire complex shapes is a fundamental question in biology and regenerative medicine. Zebrafish semicircular canals form from invaginations in the otic epithelium (buds) that extend and fuse to form the hubs of each canal. We find that conventional actomyosin-driven behaviors are not required. Instead, local secretion of hyaluronan, made by the enzymes uridine 5′-diphosphate dehydrogenase (ugdh) and hyaluronan synthase 3 (has3), drives canal morphogenesis. Charged hyaluronate polymers osmotically swell with water and generate isotropic extracellular pressure to deform the overlying epithelium into buds. The mechanical anisotropy needed to shape buds into tubes is conferred by a polarized distribution of actomyosin and E-cadherin-rich membrane tethers, which we term cytocinches. Most work on tissue morphogenesis ascribes actomyosin contractility as the driving force, while the extracellular matrix shapes tissues through differential stiffness. Our work inverts this expectation. Hyaluronate pressure shaped by anisotropic tissue stiffness may be a widespread mechanism for powering morphological change in organogenesis and tissue engineering.},
  author       = {Munjal, Akankshi and Hannezo, Edouard B and Tsai, Tony Y.C. and Mitchison, Timothy J. and Megason, Sean G.},
  issn         = {1097-4172},
  journal      = {Cell},
  number       = {26},
  pages        = {6313--6325.e18},
  publisher    = {Elsevier ; Cell Press},
  title        = {{Extracellular hyaluronate pressure shaped by cellular tethers drives tissue morphogenesis}},
  doi          = {10.1016/j.cell.2021.11.025},
  volume       = {184},
  year         = {2021},
}

@article{7001,
  author       = {Schwayer, Cornelia and Shamipour, Shayan and Pranjic-Ferscha, Kornelija and Schauer, Alexandra and Balda, M and Tada, M and Matter, K and Heisenberg, Carl-Philipp J},
  issn         = {1097-4172},
  journal      = {Cell},
  number       = {4},
  pages        = {937--952.e18},
  publisher    = {Cell Press},
  title        = {{Mechanosensation of tight junctions depends on ZO-1 phase separation and flow}},
  doi          = {10.1016/j.cell.2019.10.006},
  volume       = {179},
  year         = {2019},
}

@article{6877,
  author       = {Kopf, Aglaja and Sixt, Michael K},
  issn         = {1097-4172},
  journal      = {Cell},
  number       = {1},
  pages        = {51--53},
  publisher    = {Elsevier},
  title        = {{The neural crest pitches in to remove apoptotic debris}},
  doi          = {10.1016/j.cell.2019.08.047},
  volume       = {179},
  year         = {2019},
}

@article{9458,
  abstract     = {Dnmt1 epigenetically propagates symmetrical CG methylation in many eukaryotes. Their genomes are typically depleted of CG dinucleotides because of imperfect repair of deaminated methylcytosines. Here, we extensively survey diverse species lacking Dnmt1 and show that, surprisingly, symmetrical CG methylation is nonetheless frequently present and catalyzed by a different DNA methyltransferase family, Dnmt5. Numerous Dnmt5-containing organisms that diverged more than a billion years ago exhibit clustered methylation, specifically in nucleosome linkers. Clustered methylation occurs at unprecedented densities and directly disfavors nucleosomes, contributing to nucleosome positioning between clusters. Dense methylation is enabled by a regime of genomic sequence evolution that enriches CG dinucleotides and drives the highest CG frequencies known. Species with linker methylation have small, transcriptionally active nuclei that approach the physical limits of chromatin compaction. These features constitute a previously unappreciated genome architecture, in which dense methylation influences nucleosome positions, likely facilitating nuclear processes under extreme spatial constraints.},
  author       = {Huff, Jason T. and Zilberman, Daniel},
  issn         = {1097-4172},
  journal      = {Cell},
  number       = {6},
  pages        = {1286--1297},
  publisher    = {Elsevier},
  title        = {{Dnmt1-independent CG methylation contributes to nucleosome positioning in diverse eukaryotes}},
  doi          = {10.1016/j.cell.2014.01.029},
  volume       = {156},
  year         = {2014},
}

@article{9459,
  abstract     = {Nucleosome remodelers of the DDM1/Lsh family are required for DNA methylation of transposable elements, but the reason for this is unknown. How DDM1 interacts with other methylation pathways, such as small-RNA-directed DNA methylation (RdDM), which is thought to mediate plant asymmetric methylation through DRM enzymes, is also unclear. Here, we show that most asymmetric methylation is facilitated by DDM1 and mediated by the methyltransferase CMT2 separately from RdDM. We find that heterochromatic sequences preferentially require DDM1 for DNA methylation and that this preference depends on linker histone H1. RdDM is instead inhibited by heterochromatin and absolutely requires the nucleosome remodeler DRD1. Together, DDM1 and RdDM mediate nearly all transposon methylation and collaborate to repress transposition and regulate the methylation and expression of genes. Our results indicate that DDM1 provides DNA methyltransferases access to H1-containing heterochromatin to allow stable silencing of transposable elements in cooperation with the RdDM pathway.},
  author       = {Zemach, Assaf and Kim, M. Yvonne and Hsieh, Ping-Hung and Coleman-Derr, Devin and Eshed-Williams, Leor and Thao, Ka and Harmer, Stacey L. and Zilberman, Daniel},
  issn         = {1097-4172},
  journal      = {Cell},
  number       = {1},
  pages        = {193--205},
  publisher    = {Elsevier},
  title        = {{The Arabidopsis nucleosome remodeler DDM1 allows DNA methyltransferases to access H1-containing heterochromatin}},
  doi          = {10.1016/j.cell.2013.02.033},
  volume       = {153},
  year         = {2013},
}