Catálogo de publicaciones - libros
Reviews of Physiology Biochemistry and Pharmacology
S. G. Amara ; E. Bamberg ; S. Grinstein ; S. C. Hebert ; R. Jahn ; W. J. Lederer ; R. Lill ; A. Miyajima ; H. Murer ; S. Offermanns ; G. Schultz ; M. Schweiger (eds.)
Resumen/Descripción – provisto por la editorial
No disponible.
Palabras clave – provistas por la editorial
Human Physiology
Disponibilidad
| Institución detectada | Año de publicación | Navegá | Descargá | Solicitá |
|---|---|---|---|---|
| No detectada | 2005 | SpringerLink |
Información
Tipo de recurso:
libros
ISBN impreso
978-3-540-28192-4
ISBN electrónico
978-3-540-28217-4
Editor responsable
Springer Nature
País de edición
Reino Unido
Fecha de publicación
2005
Información sobre derechos de publicación
© Springer-Verlag Berlin Heidelberg 2005
Cobertura temática
Tabla de contenidos
Polypeptide chain termination and stop codon readthrough on eukaryotic ribosomes
S. Rospert; M. Rakwalska; Y. Dubaquié
During protein translation, a variety of quality control checks ensure that the resulting polypeptides deviate minimally from their genetic encoding template. Translational fidelity is central in order to preserve the function and integrity of each cell. Correct termination is an important aspect of translational fidelity, and a multitude of mechanisms and players participate in this exquisitely regulated process. This review explores our current understanding of eukaryotic termination by highlighting the roles of the different ribosomal components as well as termination factors and ribosome-associated proteins, such as chaperones.
Pp. 1-30
Novel roles of aquaporins revealed by phenotype analysis of knockout mice
A. S. Verkman
The aquaporins (AQPs) are small integral membrane proteins that transport water and in some cases small solutes such as glycerol. Physiological roles of the ten or more mammalian AQPs have been proposed based on their expression in epithelial, endothelial and other tissues, their regulation, and in some cases the existence of humans with AQP mutation. Here, the role of AQPs in mammalian physiology is reviewed, based on phenotype analysis of transgenic mouse models of AQP deletion/mutation. Phenotype studies support the predicted roles of AQPs in kidney tubule and microvessel fluid transport for urinary concentrating function, and in fluid-secreting glandular epithelia. The phenotype studies have also shown unexpected roles of AQPs in brain and corneal swelling, in neural signal transduction, in regulation of intracranial and intraocular pressure, and in tumor angiogenesis and cell migration. The water/glycerol-transporting AQPs were found to play unexpected roles in skin hydration and in fat metabolism. However, many phenotype studies were negative, such as normal airway/lung and skeletal muscle function, despite AQP expression, indicating that tissue-specific AQP expression does not indicate physiological significance. The mouse phenotype data suggest that modulators of AQP expression/function may have such wide-ranging clinical applications as diuretics and in the treatment of brain swelling, glaucoma, epilepsy, obesity, and cancer.
Pp. 31-55
Activation of heterotrimeric G-proteins independent of a G-protein coupled receptor and the implications for signal processing
M. J. Cismowski; S. M. Lanier
Heterotrimeric G-proteins are key transducers for signal transfer from outside the cell, mediating signals emanating from cell-surface G-protein coupled receptors (GPCR). Many, if not all, subtypes of heterotrimeric G-proteins are also regulated by accessory proteins that influence guanine nucleotide binding, guanosine triphosphate (GTP) hydrolysis, or subunit interactions. One subgroup of such accessory proteins (activators of G-protein signaling; AGS proteins) refer to a functionally defined group of proteins that activate selected G-protein signaling systems in the absence of classical G-protein coupled receptors. AGS and related proteins provide unexpected insights into the regulation of the G-protein activation-deactivation cycle. Different AGS proteins function as guanine nucleotide exchange factors or guanine nucleotide dissociation inhibitors and may also influence subunit interactions by interaction with Gβγ. These proteins play important roles in the generation or positioning of signaling complexes and of the regulation of GPCR signaling, and as alternative binding partners for G-protein subunits. Perhaps of even broader impact is the discovery that AGS proteins provide a foundation for the concept that heterotrimeric G-protein subunits are processing signals within the cell involving intrinsic cues that do not involve the classical signal input from a cell surface GPCR.
Pp. 57-80