scholarly journals UDP-Sugars as Extracellular Signaling Molecules: Cellular and Physiologic Consequences of P2Y14 Receptor Activation

2015 ◽  
Vol 88 (1) ◽  
pp. 151-160 ◽  
Author(s):  
Eduardo R. Lazarowski ◽  
T. Kendall Harden
Keyword(s):  
Receptor Activation ◽  
Signaling Molecules ◽  
Extracellular Signaling

Initiation of the proximodistal axis in insect legs

Development ◽  
1995 ◽  
Vol 121 (3) ◽  
pp. 619-628 ◽  
Author(s):  
G. Campbell ◽  
A. Tomlinson
Keyword(s):  
Protein Expression ◽  
Close Association ◽  
Cell Communication ◽  
Signaling Molecules ◽  
Cell Fates ◽  
Animal Development ◽  
Extracellular Signaling ◽  
Cell Cell

Much of the cell-cell communication that controls assignment of cell fates during animal development appears to be mediated by extracellular signaling molecules. The formation of the proximodistal (P/D) axis of the legs of flies is controlled by at least two such molecules, a Wnt and a TGFbeta, encoded by the wingless (wg) and decapentaplegic (dpp) genes, respectively. The P/D axis appears to be initiated from the site where cells expressing wg are in close association with those expressing dpp. Support for this hypothesis comes from two sources: classical grafting experiments in cockroaches and ectopic protein expression in Drosophila.

scholarly journals RNAs as extracellular signaling molecules

2008 ◽  
Vol 40 (4) ◽  
pp. 151-159 ◽  
Author(s):  
Marcel E Dinger ◽  
Timothy R Mercer ◽  
John S Mattick
Keyword(s):  
Small Molecules ◽  
Information Transfer ◽  
Signaling Molecules ◽  
Specific Information ◽  
Paracrine Signaling ◽  
Epigenetic Memory ◽  
Extracellular Signaling ◽  
Rna Signaling

RNA is emerging as a major component of the regulatory circuitry that underpins the development and physiology of complex organisms. Here we review recent evidence that suggests that RNA may supplement endocrine and paracrine signaling by small molecules and proteins, and act as an efficient and evolutionarily flexible source of sequence-specific information transfer between cells, both locally and systemically. As such, RNA signaling may play a central but previously hidden role in multicellular ontogeny, homeostasis, and transmitted epigenetic memory.

scholarly journals c-Cbl-Mediated Regulation of LAT-Nucleated Signaling Complexes

2007 ◽  
Vol 27 (24) ◽  
pp. 8622-8636 ◽  
Author(s):  
Lakshmi Balagopalan ◽  
Valarie A. Barr ◽  
Connie L. Sommers ◽  
Mira Barda-Saad ◽  
Amrita Goyal ◽  
...  
Keyword(s):  
Fluorescent Protein ◽  
Yellow Fluorescent Protein ◽  
Cell Receptor ◽  
Receptor Activation ◽  
Signaling Molecules ◽  
Endocytic Machinery ◽  
Intracellular Compartments ◽  
Tcr Activation ◽  
Mutant Forms ◽  
Multiple Signaling

ABSTRACT The engagement of the T-cell receptor (TCR) causes the rapid recruitment of multiple signaling molecules into clusters with the TCR. Upon receptor activation, the adapters LAT and SLP-76, visualized as chimeric proteins tagged with yellow fluorescent protein, transiently associate with and then rapidly dissociate from the TCR. Previously, we demonstrated that after recruitment into signaling clusters, SLP-76 is endocytosed in vesicles via a lipid raft-dependent pathway that requires the interaction of the endocytic machinery with ubiquitylated proteins. In this study, we focus on LAT and demonstrate that signaling clusters containing this adapter are internalized into distinct intracellular compartments and dissipate rapidly upon TCR activation. The internalization of LAT was inhibited in cells expressing versions of the ubiquitin ligase c-Cbl mutated in the RING domain and in T cells from mice lacking c-Cbl. Moreover, c-Cbl RING mutant forms suppressed LAT ubiquitylation and caused an increase in cellular LAT levels, as well as basal and TCR-induced levels of phosphorylated LAT. Collectively, these data indicate that following the rapid formation of signaling complexes upon TCR stimulation, c-Cbl activity is involved in the internalization and possible downregulation of a subset of activated signaling molecules.

scholarly journals Evolution and Classification of Cystine Knot-Containing Hormones and Related Extracellular Signaling Molecules

2001 ◽  
Vol 15 (5) ◽  
pp. 681-694 ◽  
Author(s):  
Ursula A. Vitt ◽  
Sheau Y. Hsu ◽  
Aaron J. W. Hsueh
Keyword(s):  
Signaling Molecules ◽  
Cystine Knot ◽  
Extracellular Signaling

scholarly journals The Mechanism of Endogenous Receptor Activation Functionally Distinguishes Prototype Canonical and Noncanonical Wnts

2005 ◽  
Vol 25 (9) ◽  
pp. 3475-3482 ◽  
Author(s):  
Guizhong Liu ◽  
Anna Bafico ◽  
Stuart A. Aaronson
Keyword(s):  
Signaling Pathways ◽  
Mammalian Cells ◽  
Receptor Activation ◽  
Signaling Molecules ◽  
Canonical Pathway ◽  
Human Diseases ◽  
Functional Interaction ◽  
Wnt Pathways

ABSTRACT Wnt glycoproteins are developmentally essential signaling molecules, and lesions afflicting Wnt pathways play important roles in human diseases. Some Wnts signal to the canonical pathway by stabilizing β-catenin, while others lack this activity. Frizzled serpentine receptors mediate distinct signaling pathways by both classes of Wnts. Here, we tandemly linked noncanonical Wnt5a with the C-terminal half of Dickkopf-2 (Dkk2C), a distinct ligand of the Wnt coreceptor LRP5/6. Whereas Wnt5a, Dkk2C, or both together were incapable of stimulating endogenous canonical signaling, the Wnt5a/Dkk2C chimera efficiently activated this pathway in a manner inhibitable by specific antagonists of either frizzled or LRP receptors. Thus, activation of the canonical pathway requires ligand coupling of an endogenous frizzled/LRP coreceptor complex, rather than Wnt triggering each receptor independently. Moreover, fusion of Wnt5a with Dkk2C unmasked its ability to signal to Dishevelled through multiple frizzleds, indicating that the lack of functional interaction with LRP distinguishes noncanonical Wnt5a from canonical Wnts in mammalian cells. These findings provide a novel mechanism by which the same receptor can be switched between distinct signaling pathways depending on the differential recruitment of a coreceptor by members of the same ligand family.

scholarly journals Gap junction modulation by extracellular signaling molecules: the thymus model

2000 ◽  
Vol 33 (4) ◽  
pp. 457-465 ◽  
Author(s):  
L.A. Alves ◽  
O.K. Nihei ◽  
P.C. Fonseca ◽  
A.C. Campos-de-Carvalho ◽  
W. Savino
Keyword(s):  
Gap Junction ◽  
Signaling Molecules ◽  
Extracellular Signaling
Sign in / Sign up

Export Citation Format

Share Document