Nature Cell Biology

doi: 10.1038/s41556-018-0103-6pmid: 29695785

Five years ago Nature Cell Biology removed word limits from Methods sections to enhance the detailed description of how experiments are designed, performed and analysed. Here, we revisit our policies that promote full transparency of methodological reporting and the reproducibility of the findings we publish.

Coller, Hilary

doi: 10.1038/s41556-018-0096-1pmid: 29662180

How the metabolic crosstalk between cancer and stromal cells affects tumour growth is incompletely defined. MYC-activated cancer cells are now shown to secrete exosomal miR-105, which fuels tumour growth by inducing a MYC-dependent metabolic programme in cancer-associated fibroblasts.

Lüders, Jens

doi: 10.1038/s41556-018-0100-9pmid: 29695790

De novo assembly of microtubules, nucleation, has remained surprisingly enigmatic, considering that microtubules are polymers of only two proteins, α- and β-tubulin, and that γ-tubulin has a well-established role as nucleator. Now, the tubulin polymerase XMAP215 is shown to be required for efficient nucleation in cooperation with γ-tubulin.

Formosa, Luke; Ryan, Michael

doi: 10.1038/s41556-018-0098-zpmid: 29662174

Mitochondria are critical for cellular energy generation and house oxidative phosphorylation (OXPHOS) complexes, which are under dual genetic control. A study finds that transcript translation and complex assembly are partitioned, and OXPHOS complexes III, IV and V are built at spatially defined regions of the mitochondrial inner membrane.

Atlasi, Yaser; Stunnenberg, Hendrik

doi: 10.1038/s41556-018-0099-ypmid: 29662177

Brd4, a reader of histone acetylation, is a transcriptional co-activator implicated in the maintenance of embryonic stem cells (ESCs). A study now shows that Brd4 is dispensable in mouse ESCs maintained in ground state pluripotency, and that cooperative activity of Tet1/2 and ESC-specific transcription factors compensates for its loss.

Inui, Masafumi; Mokuda, Sho; Sato, Tempei; Tamano, Moe; Takada, Shuji; Asahara, Hiroshi

doi: 10.1038/s41556-018-0077-4pmid: 29695789

Zou, Weiguo; Shao, Rui; Jones, Dallas

doi: 10.1038/s41556-018-0076-5pmid: 29695791

Mizushima, Noboru

doi: 10.1038/s41556-018-0092-5pmid: 29686264

The field of autophagy research has developed rapidly since the first description of the process in the 1960s and the identification of autophagy genes in the 1990s. Autophagy is now increasingly studied at the level of organismal pathophysiology and is being connected to the medical sciences. This Historical Perspective describes a brief history of autophagy and discusses unanswered cell biological questions in the field.

Stoldt, Stefan; Wenzel, Dirk; Kehrein, Kirsten; Riedel, Dietmar; Ott, Martin; Jakobs, Stefan

doi: 10.1038/s41556-018-0090-7pmid: 29662179

Oxidative phosphorylation (OXPHOS) is vital for the regeneration of the vast majority of ATP in eukaryotic cells 1 . OXPHOS is carried out by large multi-subunit protein complexes in the cristae membranes, which are invaginations of the mitochondrial inner membrane. The OXPHOS complexes are a mix of subunits encoded in the nuclear and mitochondrial genomes. Thus, the assembly of these dual-origin complexes is an enormous logistical challenge for the cell. Using super-resolution microscopy (nanoscopy) and quantitative cryo-immunogold electron microscopy, we determined where specific transcripts are translated and where distinct assembly steps of the dual-origin complexes in the yeast Saccharomyces cerevisiae occur. Our data indicate that the mitochondrially encoded proteins of complex III and complex IV are preferentially inserted in different sites of the inner membrane than those of complex V. We further demonstrate that the early, but not the late, assembly steps of complex III and complex IV occur preferentially in the inner boundary membrane. By contrast, all steps of complex V assembly occur mainly in the cristae membranes. Thus, OXPHOS complex assembly is spatially well orchestrated, probably representing an unappreciated regulatory layer in mitochondrial biogenesis.

Zhang, Yunfang; Zhang, Xudong; Shi, Junchao; Tuorto, Francesca; Li, Xin; Liu, Yusheng; Liebers, Reinhard; Zhang, Liwen; Qu, Yongcun; Qian, Jingjing; Pahima, Maya; Liu, Ying; Yan, Menghong; Cao, Zhonghong; Lei, Xiaohua; Cao, Yujing;