نتایج جستجو برای: ran

تعداد نتایج: 9987  

Journal: :Molecular biology of the cell 1997
G A Murphy M S Moore G Drivas P Pérez de la Ossa A Villamarin P D'Eustachio M G Rush

Ran, the small, predominantly nuclear GTPase, has been implicated in the regulation of a variety of cellular processes including cell cycle progression, nuclear-cytoplasmic trafficking of RNA and protein, nuclear structure, and DNA synthesis. It is not known whether Ran functions directly in each process or whether many of its roles may be secondary to a direct role in only one, for example, nu...

2010
Guillaume Bompard Gabriel Rabeharivelo Marie Frank Julien Cau Claude Delsert Nathalie Morin

Ran is an essential GTPase that controls nucleocytoplasmic transport, mitosis, and nuclear envelope formation. These functions are regulated by interaction of Ran with different partners, and by formation of a Ran-GTP gradient emanating from chromatin. Here, we identify a novel level of Ran regulation. We show that Ran is a substrate for p21-activated kinase 4 (PAK4) and that its phosphorylatio...

Journal: :JOURNAL OF INDIAN AND BUDDHIST STUDIES (INDOGAKU BUKKYOGAKU KENKYU) 1994

Journal: :Current Biology 1998
Alicia Smith Amy Brownawell Ian G. Macara

A concentration gradient of the GTP-bound form of the GTPase Ran across nuclear pores is essential for the transport of many proteins and nucleic acids between the nuclear and cytoplasmic compartments of eukaryotic cells [1] [2] [3] [4]. The mechanisms responsible for the dynamics and maintenance of this Ran gradient have been unclear. We now show that Ran shuttles between the nucleosol and cyt...

Journal: :Developmental Cell 2002

Journal: :Atlas of Genetics and Cytogenetics in Oncology and Haematology 2011

Journal: :Current Biology 2001
Chuanmao Zhang Paul R. Clarke

The molecular mechanism of nuclear envelope (NE) assembly is poorly understood, but in a cell-free system made from Xenopus eggs NE assembly is controlled by the small GTPase Ran [1,2]. In this system, Sepharose beads coated with Ran induce the formation of functional NEs in the absence of chromatin [1]. Both generation of Ran-GTP by the guanine nucleotide exchange factor RCC1 and GTP hydrolysi...

Journal: :The Journal of Cell Biology 1996
N C Chi E J Adam G D Visser S A Adam

Three factors have been identified that reconstitute nuclear protein import in a permeabilized cell assay: the NLS receptor, p97, and Ran/TC4. Ran/TC4, in turn, interacts with a number of proteins that are involved in the regulation of GTP hydrolysis or are components of the nuclear pore. Two Ran-binding proteins, RanBP1 and RanBP2, form discrete complexes with p97 as demonstrated by immunoadso...

Journal: :The Journal of Cell Biology 2002
William A. Wells

Cloning confusion very cloning pronouncement has one guaranteed ingredient: controversy. This time, Atsuo Ogura (National Institute of Infectious Diseases, Tokyo, Japan) and Rudolf Jaenisch (Massachusetts Institute of Technology, Cambridge, MA) are duking it out. Ogura claims that most of the defects that Jaenisch has seen in his cloned mice were caused by the genetic instability of the embryon...

Journal: :Biochemical Society transactions 2006
M Dasso

The Ran GTPase controls many cellular functions, including nucleocytoplasmic trafficking, spindle assembly, nuclear assembly and cell-cycle progression. Considerable evidence suggests that diffusible Ran-GTP near mitotic chromatin facilitates the release of critical factors from nuclear transport receptors, thereby promoting organization of mitotic spindles with respect to chromosomes. In addit...

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