Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain
the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in
Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles
and JavaScript.
In a recent paper published in Cell, Wang et al. report that deficiency of triggering receptor expressed on myeloid cells 2 (TREM2) augments amyloid β accumulation and neuronal loss in a mouse model of Alzheimer's disease. TREM2 acts as a signaling receptor involved in innate immunity for the natural clearance of this toxic protein by microglia.
The complexity of mechanisms driving protein sorting into exosomes is only beginning to emerge. In a paper recently published in Cell Research, Roucourt et al. report that trimming of heparan sulfate side chains of syndecans by endosomal heparanase facilitates sorting into exosomes by the formation of tight syndecan clusters that are recruited by the multivalent adaptor syntenin to the ALIX-ESCRT sorting machinery at endosomes.
Primordial germ cells (PGCs) are the earliest population of germ cells established during embryonic development and constitute the beginning of the totipotent state. A recent study provides a new protocol for the efficient generation of PGC-like cells from human embryonic stem cells, providing an in vitro platform to study human PGC differentiation and specification.
The CRISPR/Cas system has proven to be a powerful gene editing tool both in vitro and in vivo. A recent flurry of studies of in vivo gene editing using the CRISPR/Cas system bring bright prospects in creating animal models and targeted gene therapy of human genetic diseases.
The genomic and transcriptomic analysis has led to the identification of transcriptional networks that affect the differentiation of Th17 cells, while the protein-protein networks and the posttranslational modifications that control the development of Th17 cells have not been established yet. A recent publication by Rutz et al. in Nature describes a novel deubiquitylating enzyme DUBA as a negative regulator for IL-17 by regulating stability of RORγt, the master transcription factor that induces Th17 cells.