Cell Biology
- OXSR1 inhibits inflammasome activation by limiting potassium efflux during mycobacterial infection
Mycobacteria up-regulate host kinase OXSR1 preventing potassium efflux and inflammasome activation. Depletion or inhibition of OXSR1 potentiates inflammasome activation and decreases bacterial burden.
- Rab40c regulates focal adhesions and PP6 activity by controlling ANKRD28 ubiquitylation
The role of novel Rab40c/CRL5 ubiquitylation complex in regulating PP6 activity and cell migration.
- Systematic identification of ALK substrates by integrated phosphoproteome and interactome analysis
Integrated analysis of the phosphoproteome and interactome of anaplastic lymphoma kinase (ALK)-overexpressing HEK 293 cells revealed 37 ALK substrate candidates, contributing to the improvement of kinase activity prediction.
- Exploring YAP1-centered networks linking dysfunctional CFTR to epithelial–mesenchymal transition
In this work, a systems biology approach identifies potentially dysregulated EMT signaling in CF (including the Hippo, Wnt, TGF-β, p53, and MYC pathways), integrated by YAP1 and TEAD4.
- Map7D2 and Map7D1 facilitate microtubule stabilization through distinct mechanisms in neuronal cells
The microtubule-associated proteins Map7D2 and Map7D1, which belong to the MAP7 family, stabilize microtubules through distinct mechanisms for the control of cell motility and neurite outgrowth.
- Adipose tissue–specific ablation of Ces1d causes metabolic dysregulation in mice
Ces1d is a crucial enzyme in adipose tissue. Here, we found a high level of Ces1d translocates onto lipid droplets where it digests the lipids to produce unique fatty acids which are key for glucose and lipid metabolism.
- Tricalbin proteins regulate plasma membrane phospholipid homeostasis
The extended synaptotagmin (E-Syt) family are conserved proteins that function at membrane contacts. This study reveals that yeast E-Syt family members regulate phospholipid homeostasis necessary for plasma membrane integrity.
- A novel domain within the CIL regulates egress of IFITM3 from the Golgi and reveals a regulatory role of IFITM3 on the secretory pathway
In this work, it is revealed that the broad viral inhibitor IFITM3 is a previously unrecognized modulator of the functionalities of the cellular ER–Golgi secretory pathway.