Contents
Vol 2, Issue 90
Contents
Editorial Guide
- Focus Issue: The Long and Short of Redox Signaling
Reactive oxygen species mediate local and long-distance signals.
Research Articles
- Leishmania GP63 Alters Host Signaling Through Cleavage-Activated Protein Tyrosine Phosphatases
The parasite protein GP63 triggers cleavage and activation of host protein tyrosine phosphatases to promote infection.
- Hippo Pathway–Dependent and –Independent Roles of RASSF6
RASSF6 is both an inhibitor and a promoter of apoptosis, and its proapoptotic activity is regulated by the mammalian kinase MST2, a Hippo homolog.
Perspectives
- Sending ROS on a Bullet Train
Hydrogen peroxide is an auto-propagating, rapid systemic stress signal generated by RBOHD in Arabidopsis.
- STAT3 Revs Up the Powerhouse
The transcription factor STAT3 stimulates mitochondria to augment Ras-dependent oncogenic transformation.
Review
- Transduction of Redox Signaling by Electrophile-Protein Reactions
Attachment of electrophilic products of redox reactions to proteins links cell function to changes in metabolic and inflammatory status.
Editors' Choice
- Memorable microRNA
In Aplysia, long-term plasticity involves the reduction in miR-124, which increases the abundance of the transcription factor CREB1.
- Sweet Talking
Mannose- and fucose-based carbohydrates differentially modulate cytokine production in dendritic cells through their interactions with DC-SIGN.
- p53 Promotes Polarity
Loss of p53 in mammary cancer stem cells is associated with increased self-replication.
- Butterfly Navigation
Monarch butterfly antennae contain the timing mechanism for time-compensated Sun compass orientation.
- Differentiated with ROS
Reactive oxygen species contribute to blood cell specification in flies.
- Stimulating H+ Efflux to Promote Reorganization
Akt-dependent phosphorylation and activation of NHE1 is critical to growth factor–dependent reorganization of the actin cytoskeleton.
- Cataloging Kinase Targets
Cell signaling may be understood in terms of the evolution of the topology and distribution of protein phosphorylation sites.