Journal ArticleDOI
The GTPase superfamily: a conserved switch for diverse cell functions
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TLDR
A molecular switch is a molecular switch whose "on" and "off" states are triggered by binding and hydrolysis of GTP as discussed by the authors. But the mechanism in myriad versions of the switch can be traced back to a single primordial protein.Abstract:
Proteins that bind and hydrolyse GTP are being discovered at a rapidly increasing rate. Each of these many GTPases acts as a molecular switch whose 'on' and 'off' states are triggered by binding and hydrolysis of GTP. Conserved structure and mechanism in myriad versions of the switch--in bacteria, yeast, flies and vertebrates--suggest that all derive from a single primordial protein, repeatedly modified in the course of evolution to perform a dazzling variety of functions.read more
Citations
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Journal ArticleDOI
The GTPase superfamily: conserved structure and molecular mechanism
TL;DR: GTPases are conserved molecular switches, built according to a common structural design, and rapidly accruing knowledge of individual GTPases—crystal structures, biochemical properties, or results of molecular genetic experiments—support and generate hypotheses relating structure to function in other members of the diverse family of GTPase.
Journal ArticleDOI
Cancer metastasis and angiogenesis: an imbalance of positive and negative regulation.
TL;DR: General themes are emerging that yield new strategies for prognosis and therapy of hu- man metastatic cancer, and an imbalanced regulation of motility and proteoly- sis appears to be required for invasion and metastasis.
Journal ArticleDOI
Small GTP-Binding Proteins
TL;DR: In this review, functions of small G proteins and their modes of activation and action are described.
Journal ArticleDOI
Identification of FAP locus genes from chromosome 5q21
Kenneth W. Kinzler,Mef Nilbert,Li Kuo Su,Bert Vogelstein,Tracy M. Bryan,Daniel B. Levy,Kelly J. Smith,Antonette C. Preisinger,Hedge Philip John,Douglas McKechnie,Rachel Finniear,Alex Markham,John Groffen,Mark S. Boguski,Stephen F. Altschul,Akira Horii,Hiroshi Ando,Yasuo Miyoshi,Yoshio Miki,Isamu Nishisho,Yusuke Nakamura +20 more
TL;DR: The APC gene was identified in a contig initiated from the MCC gene and was found to encode an unusually large protein, and these two closely spaced genes encode proteins predicted to contain coiled-coil regions, which were also expressed in a wide variety of tissues.
Journal ArticleDOI
Diversity of G proteins in signal transduction.
TL;DR: The heterotrimeric guanine nucleotide-binding proteins acting as switches that regulate information processing circuits connecting cell surface receptors to a variety of effectors generate the pathways that modulate cellular responses to complex chemical signals.
References
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Journal ArticleDOI
G proteins: transducers of receptor-generated signals
TL;DR: This paper presents a meta-analysis of G Protein Interactions and its Foundations, which states that G Proteins are Law-Regulated and G Protein-Effector Interactions are Nonvolatile.
Journal ArticleDOI
All ras proteins are polyisoprenylated but only some are palmitoylated
TL;DR: It is shown that all ras proteins are polyisoprenylated on their C-terminal cysteine (Cys186) and palmitoylation increases the avidity of this binding and enhances their transforming activity.
Journal ArticleDOI
GTPase inhibiting mutations activate the α chain of G s and stimulate adenylyl cyclase in human pituitary tumours
TL;DR: A subset of growth hormone-secreting human pituitary tumours carries somatic mutations that inhibit GTPase activity of a G protein α chain, αs, which results in the activation of adenylyl cyclase, which bypasses the cells' normal requirement for trophic hormone.
Journal ArticleDOI
Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments.
TL;DR: Findings provide evidence that members of the YPT1/SEC4 subfamily of GTP binding proteins are localized to specific exocytic and endocytic subcompartments in mammalian cells.
Journal ArticleDOI
A cytoplasmic protein stimulates normal N-ras p21 GTPase, but does not affect oncogenic mutants
Meg Trahey,Frank McCormick +1 more
TL;DR: In Xenopus oocytes, this protein maintains normal p21 in a biologically inactive, GDP-bound state through its effect on GTPase activity, and it appears that the major effect of position 12 mutations is to prevent this protein from stimulating p21 GTP enzyme activity, thereby allowing these mutants to remain in the active GTP- bound state.