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SPOTLIGHT ON KANAZAWA
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TABLE OF CONTENTS
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November 2018 Volume 19, Issue 11 |
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 |  Research Highlights
Reviews
Amendments & Corrections
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New Poster on: Epitranscriptome regulation
Download a new poster from Nature Structural & Molecular Biology on epitranscriptome regulation, a key mechanism affecting gene expression as well as cellular functions, development and disease.
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Produced with support from Accent Therapeutics, Inc. | |
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Research Highlights | |
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Transcriptionally tailored break repair
Eytan Zlotorynski
p675 | doi:10.1038/s41580-018-0069-z
DNA double-strand breaks at active genes are repaired by a dedicated homologous recombination mechanism involving R-loop formation and RAD52 recruitment.
PDF
| Disordered interactions
Paulina Strzyz
pp676 - 677 | doi:10.1038/s41580-018-0061-7
Direct demonstration that mutations in intrinsically disordered regions modulate protein–protein interaction networks, which may cause disease.
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| A(TR) checkpoint for S/G2 transition
Michelle Trenkmann
pp676 - 677 | doi:10.1038/s41580-018-0064-4
The kinase ATR senses the completion of DNA replication and controls the S/G2 cell-cycle transition.
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| HATs off for the Lasker awardees
Paulina Strzyz
p677 | doi:10.1038/s41580-018-0065-3
Nature Reviews Molecular Cell Biology congratulates the winners of the 2018 Lasker Foundation Awards.
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Reviews | |
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To degrade or not to degrade: mechanisms and significance of endocytic recycling
Peter J. Cullen & Florian Steinberg
pp679 - 696 | doi:10.1038/s41580-018-0053-7
Endocytosed membrane proteins can either be degraded in the lysosome or recycled back to the membrane. This decision, which has an impact on protein levels, spatial distribution and function, is controlled by recycling machineries at the endosome that recognize and segregate cargo destined for recycling, thereby preventing its degradation.
Full Text | PDF
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Regulation of proteasome assembly and activity in health and disease
Adrien Rousseau & Anne Bertolotti
pp697 - 712 | doi:10.1038/s41580-018-0040-z
Protein degradation by the proteasome is crucial for the control of many cellular processes, and defects in proteasomal degradation may lead to cancer and neurodegeneration. TOR complex 1 has a key role in regulating proteasome abundance and assembly and in integrating proteasomal activity with autophagy pathways and, more generally, cell physiology.
Full Text | PDF
Collection: Translation and protein quality control
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The machineries, regulation and cellular functions of mitochondrial calcium
Carlotta Giorgi, Saverio Marchi & Paolo Pinton
pp713 - 730 | doi:10.1038/s41580-018-0052-8
Uptake of Ca2+ ions by mitochondria regulates their functions and serves to buffer Ca2+ concentrations to maintain cellular Ca2+ homeostasis. Better understanding of the mechanisms, regulation and (patho)physiology of mitochondrial Ca2+ influx and efflux offers the possibility to target mitochondrial Ca2+ machineries for therapeutic benefit.
Full Text | PDF
Collection: Mitochondria
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Linking cellular stress responses to systemic homeostasis
Lorenzo Galluzzi, Takahiro Yamazaki & Guido Kroemer
pp731 - 745 | doi:10.1038/s41580-018-0068-0
Cellular stress responses primarily serve to rectify stress-associated damage. However, these responses are also coupled with the generation of various signals that are transmitted to the cellular microenvironments or even across tissues. This communication generally supports the maintenance of systemic homeostasis but can also result in pathology.
Full Text | PDF
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Amendments & Corrections | |
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Publisher Correction: The machineries, regulation and cellular functions of mitochondrial calcium
Carlotta Giorgi, Saverio Marchi & Paolo Pinton
p746 | doi:10.1038/s41580-018-0066-2
Full Text | PDF
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