The Drosophila light-activated conductance is composed of the two channels TRP and TRPL

Article Abstract:

The Drosophila light-activated conductance is constituted by the transient receptor potential (TRP) and TRP-like (TRP-L) ion-channels that have partially overlapping functions. TRPL has 40% amino acid identity with TRP. TRP and TRPL are capable of independent response to light-activation, and are coexpressed along with phospholipase C and rhodopsin in the membranes of the transducing organelles. The light-activated channels are not gated by store-operated calcium release mechanisms or cyclic guanosine monophosphate.

Physiological aspects, Electric properties, Ion channels, Membranes (Biology), Electrophysiology

---

GPCR signaling is required for blood-brain barrier formation in Drosophila

Article Abstract:

The G protein-coupled receptor (GPCR) Moody, the G protein subunits Galphai Loco are required in the surface glia to achieve effective insulation. A study demonstrates the importance of morphogenetic regulation in the blood-brain barrier development and places GPCR signaling at its core.

Science & research, Genetic aspects, G proteins, Blood-brain barrier

---

Similar abstracts:

• Abstracts: A new Bacteroides conjugative transposon that carries an ermB gene. Mapping of neutralizing epitopes on Renibacterium salmoninarum p57 by use of transposon mutagenesis and synthetic peptides
• Abstracts: Drosophila Myc regulates organ size by inducing cell competition. The molecular basis of odor coding in the Drosophila antenna
• Abstracts: Stimulation of RARalpha activation function AF-1 through binding to the general transcription factor TFIIH and phosphorylation by CDK7
• Abstracts: Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. Siah2 regulates stability of prolyl-hydroxylases, controls HIF1 alpha abundance, and modulates physiological responses to hypoxia
• Abstracts: A role for dystroglycan in basement membrane assembly. Disruption of the sarcoglycan-sarcospan complex in vascular smooth muscle: a novel mechanism for cardiomyopathy and muscular dystrophy

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.