Contents
Vol 5, Issue 243
Contents
Research Articles
- Superbinder SH2 Domains Act as Antagonists of Cell Signaling
Engineered SH2 domains with high affinity for phosphorylated tyrosine inhibit cell signaling downstream of receptor tyrosine kinases.
- Phosphorylation of Cytohesin-1 by Fyn Is Required for Initiation of Myelination and the Extent of Myelination During Development
Transgenic and knockout mice reveal a pathway that controls the extent of myelination by Schwann cells.
- The Tumor Suppressor PTEN Is Exported in Exosomes and Has Phosphatase Activity in Recipient Cells
A tumor suppressor protein with lipid phosphatase activity is carried to target cells in microvesicles.
Perspectives
- Peptide-Binding Domains: Are Limp Handshakes Safest?
Engineered high-affinity SH2 domains inhibit signaling and may be evolutionarily unfavorable.
- Where EGF Receptors Transmit Their Signals
Trafficking of activated epidermal growth factor receptors controls the transcriptional response to this oncogenic pathway.
- Cell Responses to Growth Factors: The Role of Receptor Tyrosine Kinase Intracellular Domain Fragments
Proteolysis of receptor tyrosine kinases produces intracellular fragments with distinct roles in growth factor signaling.
Editors' Choice
- iNKT Cells Reduce Obesity
Invariant natural killer T cells produce anti-inflammatory cytokines in the adipose tissue and protect against diet-induced obesity.
- Neutrophils Suppress Insulin Signaling
Neutrophils secrete elastase, which not only recruits other immune cells but also inhibits insulin signaling in adipose and liver.
- Virulence Through Cysteine Phosphorylation
Reversible phosphorylation of cysteine regulates the DNA binding activity of a virulence protein in Staphylococcus aureus.
- Peroxide Promotes Survival
In Caenorhabditis elegans, hydrogen peroxide can stimulate the transcriptional activation of genes involved in lipid biosynthesis.
