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14-3-3 proteins and signal transduction

Ferl, R.J. (University of Florida, Gainesville, FL.)

Annual review of plant physiology and plant molecular biology, 1996-06, Vol.47 (1), p.49-73

United States

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Título:
14-3-3 proteins and signal transduction
Autor: Ferl, R.J. (University of Florida, Gainesville, FL.)
Assuntos: BIOCHEMICAL PATHWAYS ; CHEMICAL REACTIONS ; EVOLUCION ; EVOLUTION ; FISIOLOGIA VEGETAL ; FONCTION PHYSIOLOGIQUE ; FOSFORILACION ; FUNCION FISIOLOGICA ; GENETICA ; GENETICS ; GENETIQUE ; HISTOIRE ; HISTORIA ; HISTORY ; INTERACTIONS ; LITERATURE REVIEWS ; PHOSPHORYLATION ; PHYSIOLOGICAL FUNCTIONS ; PHYSIOLOGIE VEGETALE ; PLANT PHYSIOLOGY ; PLANT PROTEINS ; PROTEIN KINASE ; PROTEINA QUINASA ; PROTEINE KINASE ; REACCIONES QUIMICAS ; REACTION CHIMIQUE ; VIA BIOQUIMICA DEL METABOLISMO ; VOIE BIOCHIMIQUE DU METABOLISME
É parte de: Annual review of plant physiology and plant molecular biology, 1996-06, Vol.47 (1), p.49-73
Notas: F60
9620235
B50
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Descrição: Perhaps in keeping with their enigmatic name, 14-3-3 proteins offer a seemingly bewildering array of opportunities for interaction with signal transduction pathways. In each organism there are many isoforms that can form both homo- and heterodimers, and many biochemical activities have been attributed to the 14-3-3 group. The potential for diversity-and also confusion-is high. The mammalian literature on 14-3-3 proteins provides an appropriate context to appreciate the potential roles of 14-3-3s in plant signal transduction pathways. In addition, functional and structural themes emerge when 14-3-3s are examined and compiled in ways that draw attention to their participation in protein phosphorylation and protein-protein interactions. These themes allow examination of plant 14-3-3s from two perspectives: the ways in which plant 14-3- 3s contribute to and extend ideas already described in animals, and the ways that plant 14-3-3s present unique contributions to the field. The crystal structure of an animal 14-3- 3 has been solved. When considered with the evolutionary stability of large segments of the 14-3-3 protein, the structure illuminates several aspects of 14-3-3 function. However, diversity in other regions of the 14-3-3s and their presence as multigene families offer many opportunities for cell-specific specialization of individual functions.
Editor: United States
Idioma: Inglês

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14-3-3 proteins and signal transduction

Ferl, R.J. (University of Florida, Gainesville, FL.)

United States

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