Cell Adhesion, Polarity & Cytoskeleton
- PlexinD1 signaling controls morphological changes and migration termination in newborn neurons
- Masato Sawada1,
- Nobuhiko Ohno2,3,
- Mitsuyasu Kawaguchi4,
- Shih‐hui Huang1,
- Takao Hikita1,
- Youmei Sakurai1,
- Huy Bang Nguyen2,
- Truc Quynh Thai2,
- Yuri Ishido1,
- Yutaka Yoshida5,
- Hidehiko Nakagawa4,
- Akiyoshi Uemura6 and
- Kazunobu Sawamoto (sawamoto{at}med.nagoya-cu.ac.jp)*,1,7
- 1Department of Developmental and Regenerative Biology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Japan
- 2Division of Neurobiology and Bioinformatics, National Institute for Physiological Sciences, Okazaki, Japan
- 3Department of Anatomy, Division of Histology and Cell Biology, Jichi Medical University, School of Medicine, Shimotsuke, Japan
- 4Department of Organic and Medicinal Chemistry, Nagoya City University Graduate School of Pharmaceutical Sciences, Nagoya, Japan
- 5Division of Developmental Biology, Cincinnati Children's Hospital Medical Center, Cincinnati, OH, USA
- 6Department of Retinal Vascular Biology, Nagoya City University Graduate School of Medical Sciences, Nagoya, Japan
- 7Division of Neural Development and Regeneration, National Institute for Physiological Sciences, Okazaki, Japan
- ↵*Corresponding author. Tel: +81 52 853 8532; Fax: +81 52 851 1898; E‐mail: sawamoto{at}med.nagoya-cu.ac.jp
Migrating olfactory neurons extend a filopodium‐like lateral protrusion to terminate neuronal migration at the correct position in the olfactory bulb via Sema3E‐PlexinD1‐Rac1 signaling.
Synopsis
During termination of neuronal migration, newborn neurons are found to transiently extend a protrusion termed filopodium‐like lateral protrusion (FLP). PlexinD1 signaling controls the FLP formation and migration termination of newborn neurons through regulation of microtubule dynamics.
Migrating neurons transiently extend an FLP during neuronal deceleration.
The FLP formation is induced by PlexinD1 downregulation and local Rac1 activation.
Microtubule polymerization within the FLP suppresses the somal translocation of newborn neurons.
PlexinD1 signaling determines the final positioning, dendritic patterns, and function of new neurons in the olfactory bulb.
The EMBO Journal (2018) 37: e97404
- Received May 19, 2017.
- Revision received October 28, 2017.
- Accepted December 15, 2017.
- © 2018 The Authors
- Miro proteins coordinate microtubule‐ and actin‐dependent mitochondrial transport and distribution
- Guillermo López‐Doménech1,
- Christian Covill‐Cooke1,
- Davor Ivankovic1,
- Els F Halff1,
- David F Sheehan1,
- Rosalind Norkett1,
- Nicol Birsa1 and
- Josef T Kittler (j.kittler{at}ucl.ac.uk)*,1
- ↵*Corresponding author. Tel: +44 (0) 2076793218; E‐mail: j.kittler{at}ucl.ac.uk
In addition to controlling mitochondrial retrograde trafficking along microtubules, Miro GTPases also mediate actin‐dependent movements via recruitment of mitochondrial myosin 19.
Synopsis
Miro1 and Miro2 coordinate specific and overlapping functions to regulate microtubule‐ and actin‐dependent mitochondrial trafficking. This coordination is critical to ensure correct mitochondrial segregation during cell division.
Miro proteins are differentially required in different stages of embryonic development.
Miro proteins are not essential for TRAK/kinesin‐mediated anterograde mitochondrial movement.
Miro1 regulates TRAK2‐dependent mitochondrial retrograde transport.
Miro proteins recruit and stabilize mitochondrial myosin Myo19 on the outer mitochondrial membrane to mediate actin‐based mitochondrial movements.
Miro proteins coordinate tubulin‐ and actin‐mediated mitochondrial movement to regulate equal segregation of mitochondria during mitosis.
The EMBO Journal (2018) 37: 321–336
- Received December 22, 2016.
- Revision received November 24, 2017.
- Accepted December 4, 2017.
- © 2018 The Authors. Published under the terms of the CC BY 4.0 license
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- WH2 and proline‐rich domains of WASP‐family proteins collaborate to accelerate actin filament elongation
- Peter Bieling (peter.bieling{at}mpi-dortmund.mpg.de)*,1,2,3,6,†,
- Scott D Hansen1,7,†,
- Orkun Akin1,8,
- Tai‐De Li2,3,4,9,
- Carl C Hayden5,10,
- Daniel A Fletcher (fletch{at}berkeley.edu)*,2,3,4 and
- R Dyche Mullins (dyche.mullins{at}ucsf.edu)*,1
- 1Department of Cellular and Molecular Pharmacology and Howard Hughes Medical Institute, University of California, San Francisco, CA, USA
- 2Department of Bioengineering & Biophysics Program, University of California, Berkeley, CA, USA
- 3Chan Zuckerberg Biohub, San Francisco, CA, USA
- 4Biological Systems & Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA, USA
- 5Sandia National Laboratories, Livermore, CA, USA
- 6Present Address: Department of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund, Germany
- 7Present Address: Department of Chemistry and Biochemistry, University of Oregon, Eugene, OR, USA
- 8Present Address: Department of Biological Chemistry, University of California, Los Angeles, CA, USA
- 9Present Address: Advanced Science Research Center, City University of New York, New York, NY, USA
- 10Present Address: Department of Biomedical Engineering, The University of Texas at Austin, Austin, TX, USA
- ↵*
Corresponding author: Tel: +49 0231 133 2248; E‐mail: peter.bieling{at}mpi-dortmund.mpg.de
Corresponding author: Tel: +1 510 664 4404; E‐mail: fletch{at}berkeley.edu
Corresponding author: Tel: +1 415 502 4838; E‐mail: dyche.mullins{at}ucsf.edu
↵† These authors contributed equally to this work
In addition to creating new actin filaments via the Arp2/3 complex, WASP‐family proteins promote actin filament growth by recruiting actin monomers and actin‐profilin complexes to membrane surfaces.
Synopsis
WASP‐family proteins activate the Arp2/3 complex to create new actin filaments in branched networks. New data show that these proteins also accelerate elongation of nearby filaments by providing a source of polymerization‐competent actin.
Polymerase activity of WASP‐family proteins arises from the recruitment of actin monomers and profilin‐actin complexes to surfaces containing a high density of WASP‐family proteins.
Most actin subunits enter a branched filament network via the WASP‐family protein‐coated surface and not directly from solution.
Profilin controls whether an actin monomer interacts with the WH2 or the proline‐rich domain of WASP family proteins.
Coordination between Proline‐rich and WH2 sequences sets the balance between the network polymerase and tethering activity of WASP family proteins.
The EMBO Journal (2018) 37: 102–121
- Received March 29, 2017.
- Revision received September 19, 2017.
- Accepted September 20, 2017.
- © 2017 The Authors. Published under the terms of the CC BY 4.0 license
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Combinatorial regulation of the balance between dynein microtubule end accumulation and initiation of directed motility
- Rupam Jha1,2,
- Johanna Roostalu1,
- Nicholas I Cade1,
- Martina Trokter1,3 and
- Thomas Surrey (thomas.surrey{at}crick.ac.uk)*,1
- 1The Francis Crick Institute, London, UK
- 2Present Address: Discovery Sciences, Innovative Medicines and Early Development, AstraZeneca, Cambridge, UK
- 3Present Address: Centre for Therapeutics Discovery, MRC Technology SBC Open Innovation Campus, Stevenage, UK
- ↵*Corresponding author. Tel: +44 2037962044; E‐mail: thomas.surrey{at}crick.ac.uk
In vitro reconstitution of the human dynein complex reveals the differential control of dynein activity on dynamic microtubules by a combination of its key regulators.
Synopsis
The balance between processive minus‐end directed motility and microtubule plus‐end localisation of dynein is controlled by various regulatory proteins. In vitro reconstitutions of the human dynein complex in the presence of end binding proteins reveal the differential control of dynein activity on dynamic microtubules by a combination of its key regulators.
Processively moving and plus end tracking dynein pools both contain dynactin, but show otherwise distinct preferences for binding regulators.
Dynactin recruits dynein to microtubule plus ends in the presence, and—to a lesser extent—also in the absence of EB1.
BicD2 is necessary for initiating processive minus‐end directed motility of the dynein/dynactin complex.
Dynactin causes a bias of dynein motility initiation from microtubule plus ends.
Lis1 has a dual role in the initiation of dynein/dynactin processive motility and microtubule plus end recruitment.
The EMBO Journal (2017) 36: 3387–3404
- Received April 4, 2017.
- Revision received September 4, 2017.
- Accepted September 13, 2017.
- © 2017 The Francis Crick Institute Limited. Published under the terms of the CC BY 4.0 license
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- Initiation of DNA replication requires actin dynamics and formin activity
- Nikolaos Parisis1,2,6,†,
- Liliana Krasinska1,†,
- Bethany Harker1,7,
- Serge Urbach3,
- Michel Rossignol2,
- Alain Camasses1,
- James Dewar4,
- Nathalie Morin5 and
- Daniel Fisher (daniel.fisher{at}igmm.cnrs.fr)*,1
- 1IGMM, CNRS Univ. Montpellier, Montpellier, France
- 2Laboratory of Functional Proteomics, INRA, Montpellier, France
- 3Functional Proteomics Platform (FPP), Institute of Functional Genomics (IGF), CNRS UMR 5203 INSERM U661, Montpellier, France
- 4Vanderbilt University, Nashville, TN, USA
- 5CRBM, CNRS Univ. Montpellier, Montpellier, France
- 6Present Address: Institut Jacques Monod, CNRS UMR7592 University Paris Diderot, Paris, France
- 7Present Address: Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK
- ↵*Corresponding author. Tel: +33 434 359 964; E‐mail: daniel.fisher{at}igmm.cnrs.fr
↵† These authors contributed equally to this work
Regulation of actin dynamics affects DNA synthesis in human cells and Xenopus egg extracts through multiple mechanisms, including nuclear transport and chromatin loading of replication factors.
Synopsis
Regulation of actin dynamics affects both the initiation and elongation steps of DNA replication in human cells and Xenopus egg extracts, through various mechanisms including nuclear transport and chromatin loading of replication factors.
Nuclear actin dynamics are required for DNA replication in embryonic and somatic cell systems.
Disrupting actin dynamics or inhibiting formin proteins blocks nuclear transport.
Nuclear actin interactions with RanGTP–importin complexes control cargo release.
Nuclear formin activity promotes chromatin localisation of replication factors.
The EMBO Journal (2017) 36: 3212–3231
- Received January 23, 2017.
- Revision received August 28, 2017.
- Accepted September 7, 2017.
- © 2017 The Authors
- KTN80 confers precision to microtubule severing by specific targeting of katanin complexes in plant cells
- Chaofeng Wang1,2,†,
- Weiwei Liu1,2,†,
- Guangda Wang1,2,†,
- Jun Li2,3,
- Li Dong1,
- Libo Han1,
- Qi Wang1,
- Juan Tian1,
- Yanjun Yu1,
- Caixia Gao3 and
- Zhaosheng Kong (zskong{at}im.ac.cn)*,1
- 1State Key Laboratory of Plant Genomics, Institute of Microbiology, Chinese Academy of Sciences, Beijing, China
- 2University of Chinese Academy of Sciences, Beijing, China
- 3State Key Laboratory of Plant Cell and Chromosome Engineering, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China
- ↵*Corresponding author. Tel/Fax: +86 10 6480 6099; E‐mail: zskong{at}im.ac.cn
↵† These authors contributed equally to this work
Microtubule‐severing complex katanin is guided to crossover and branching nucleation sites by subunit p80, which in turn recruits the catalytic subunit p60.
Synopsis
The Arabidopsis thaliana katanin p80 subunit KTN80 plays a crucial role in defining the site of microtubule severing by precisely targeting katanin complex to microtubule crossover and branching nucleation sites.
Four KTN80 isoforms act redundantly to sever microtubules at crossover and branching nucleation sites.
KTN80 targets the katanin p60 subunit KTN1 to microtubules.
KTN1 is dispensable for KTN80 recruitment to microtubules.
KTN1 is required for hexamerisation of KTN1–KTN80 heterodimers to form an active katanin complex.
The EMBO Journal (2017) 36: 3435–3447
- Received February 26, 2017.
- Revision received August 31, 2017.
- Accepted September 8, 2017.
- © 2017 The Authors
- Centriole translocation and degeneration during ciliogenesis in Caenorhabditis elegans neurons
- Wenjing Li1,
- Peishan Yi1,
- Zhiwen Zhu1,
- Xianliang Zhang1,
- Wei Li1 and
- Guangshuo Ou (guangshuoou{at}tsinghua.edu.cn)*,1
- 1Tsinghua‐Peking Center for Life Sciences, School of Life Sciences and MOE Key Laboratory for Protein Science, Tsinghua University, Beijing, China
- ↵*Corresponding author. Tel: +86 10 62794766; E‐mail: guangshuoou{at}tsinghua.edu.cn
Cilia formation in Caenorhabditis elegans sensory neurons involves dynein‐mediated centriole transport into growing dendrites, followed by sequential loss of central tube components.
Synopsis
Ciliogenesis in Caenorhabditis elegans sensory neurons requires dynein‐1‐dependent dendritic translocation of the centriole to position centriole‐derived basal body that forms a template for cilium formation.
The centriole is transported from neuronal body to the tip of the dendrite before cilium assembly.
The centriolar protein SAS‐5 interacts with the dynein light chain LC8.
Conditional mutations of dynein‐1 block centriole translocation and ciliogenesis.
Translocated centrioles lose central tube components and subsequently recruit transition zone and intraflagellar transport proteins.
The EMBO Journal (2017) 36: 2553–2566
- Received March 6, 2017.
- Revision received June 6, 2017.
- Accepted July 3, 2017.
- © 2017 The Authors
- Tumor matrix stiffness promotes metastatic cancer cell interaction with the endothelium
- Steven E Reid1,
- Emily J Kay1,
- Lisa J Neilson1,
- Anne‐Theres Henze2,
- Jens Serneels2,
- Ewan J McGhee1,
- Sandeep Dhayade1,
- Colin Nixon1,
- John BG Mackey1,3,
- Alice Santi1,
- Karthic Swaminathan1,
- Dimitris Athineos1,
- Vasileios Papalazarou1,4,
- Francesca Patella1,
- Álvaro Román‐Fernández5,
- Yasmin ElMaghloob1,
- Juan Ramon Hernandez‐Fernaud1,
- Ralf H Adams6,
- Shehab Ismail1,
- David M Bryant1,5,
- Manuel Salmeron‐Sanchez4,
- Laura M Machesky1,
- Leo M Carlin1,
- Karen Blyth1,
- Massimiliano Mazzone2,7 and
- Sara Zanivan (s.zanivan{at}beatson.gla.ac.uk)*,1,5
- 1Cancer Research UK Beatson Institute, Glasgow, UK
- 2Lab of Tumor Inflammation and Angiogenesis, Center for Cancer Biology, VIB, Leuven, Belgium
- 3Inflammation, Repair and Development, Imperial College London, London, UK
- 4Division of Biomedical Engineering, School of Engineering, University of Glasgow, Glasgow, UK
- 5Institute of Cancer Sciences, University of Glasgow, Glasgow, UK
- 6Department of Tissue Morphogenesis, Faculty of Medicine, Max‐Planck‐Institute for Molecular Biomedicine, University of Münster, Münster, Germany
- 7Lab of Tumor Inflammation and Angiogenesis, Center for Cancer Biology, Department of Oncology, KU Leuven, Leuven, Belgium
- ↵*Corresponding author. Tel: +44 141 330 3971; E‐mail: s.zanivan{at}beatson.gla.ac.uk
Quantitative mass spectrometry identifies CCN1 as the basis for matrix stiffness effects on tumor progression via mediating adhesion to endothelial cells and thereby cancer cell intravasation into the vasculature.
Synopsis
Mass spectrometric identification of CCN1 provides insight into how tumor matrix stiffness affects tumor growth and metastasis by increasing endothelial cell‐cancer cell adhesion, a key step in cancer cell intravasation into the vasculature.
Increased tumor matrix stiffness upregulates CCN1/CYR61 expression in endothelial cells.
CCN1 induces N‐cadherin expression via β‐catenin activity.
Increased N‐cadherin surface expression mediates cancer cell‐endothelium adhesion.
CCN1 deficiency in endothelial cells decreases cancer‐endothelial cell interactions in vivo.
The EMBO Journal (2017) 36: 2373–2389
- Received May 31, 2016.
- Revision received June 8, 2017.
- Accepted June 9, 2017.
- © 2017 Cancer Research UK Beatson Institute. Published under the terms of the CC BY 4.0 license
This is an open access article under the terms of the Creative Commons Attribution 4.0 License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
- PAR‐1 promotes microtubule breakdown during dendrite pruning in Drosophila
- Svende Herzmann1,
- Rafael Krumkamp1,
- Sandra Rode1,
- Carina Kintrup1 and
- Sebastian Rumpf (sebastian.rumpf{at}uni-muenster.de)*,1
- ↵*Corresponding author. Tel: +49 251 8322390; E‐mail: sebastian.rumpf{at}uni-muenster.de
Severing of unspecific neurites during neuronal morphogenesis is facilitated by PAR‐1‐mediated Tau phosphorylation, which increases microtubule dynamics prior to disassembly.
Synopsis
The developmental elimination of long stretches of neurite during neuronal morphogenesis—also known as pruning—involves the disassembly of microtubules in affected neurites. Using genetic and imaging analyses of dendrite pruning in Drosophila, we found that microtubule disruption is driven by the kinase PAR‐1, likely via an inhibitory effect on Tau.
Mutation or knockdown of PAR‐1 leads to dendrite pruning defects.
Loss of PAR‐1 prevents microtubule disruption during pruning.
PAR‐1 increases microtubule dynamics at the onset of pruning.
Genetic analysis suggests Tau is the relevant PAR‐1 target.
PAR‐1 is also required for subsequent membrane collapse.
The EMBO Journal (2017) 36: 1981–1991
- Received October 15, 2016.
- Revision received April 21, 2017.
- Accepted April 26, 2017.
- © 2017 The Authors
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