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RanGAP
RanGAP is a protein involved in the transport of other proteins from the cytosol to the nucleus in eukaryotic cells. In model species such as the yeast ''Saccharomyces cerevisiae'', the primate ''Homo sapiens'' (See RANGAP1) and the plant ''Arabidopsis thaliana,'' it acts as a GTPase-activating protein, catalysing the conversion of cytosolically-bound RanGTP to RanGDP. It has the opposite function of the RCC1, a nuclear-located protein that converts RanGDP to RanGTP. Together, RanGAP and RCC1 maintain what is known as the ran gradient, where RanGDP is in higher concentrations in the cytosol, while RanGTP is in higher concentrations in the nucleus. It is this ran gradient which provides the energy necessary for the transport of proteins into and out of the nucleus by karyopherin proteins. Location in cell In mammalian and plant cells, RanGAP is located at the nuclear envelope during interphase. Animal RanGAP is bound to the nuclear pore component RANBP2 (Nup358). Plant RanGAP protei ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RANGAP1
Ran GTPase-activating protein 1 is an enzyme that in humans is encoded by the ''RANGAP1'' gene. Function RanGAP1, is a homodimeric 65-kD polypeptide that specifically induces the GTPase activity of RAN, but not of RAS by over 1,000-fold. RanGAP1 is the immediate antagonist of RCC1, a regulator molecule that keeps RAN in the active, GTP-bound state. The RANGAP1 gene encodes a 587-amino acid polypeptide. The sequence is unrelated to that of GTPase activators for other RAS-related proteins, but is 88% identical to Rangap1 (Fug1), the murine homolog of yeast Rna1p. RanGAP1 and RCC1 control RAN-dependent transport between the nucleus and cytoplasm. RanGAP1 is a key regulator of the RAN GTP/GDP cycle. Interactions RanGAP1 is a trafficking protein which helps transport other proteins from the cytoplasm to the nucleus. Small ubiquitin-related modifier needs to be associated with it before it can be localized at the nuclear pore. RANGAP1 has been shown to interact with: * Ran, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RanGTP
Ran (RAs-related Nuclear protein) also known as GTP-binding nuclear protein Ran is a protein that in humans is encoded by the RAN gene. Ran is a small 25 kDa protein that is involved in transport into and out of the cell nucleus during interphase and also involved in mitosis. It is a member of the Ras superfamily. Ran is a small G protein that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein has also been implicated in the control of DNA synthesis and cell cycle progression, as mutations in Ran have been found to disrupt DNA synthesis. Function Ran cycle Ran exists in the cell in two nucleotide-bound forms: GDP-bound and GTP-bound. RanGDP is converted into RanGTP through the action of RCC1, the nucleotide exchange factor for Ran. RCC1 is also known as RanGEF (Ran Guanine nucleotide Exchange Factor). Ran's intrinsic GTPase-activity is activated through interaction with Ran GTPase activating protein (RanGAP), facilitat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Ran (protein)
Ran (RAs-related Nuclear protein) also known as GTP-binding nuclear protein Ran is a protein that in humans is encoded by the RAN gene. Ran is a small 25 kDa protein that is involved in transport into and out of the cell nucleus during interphase and also involved in mitosis. It is a member of the Ras superfamily. Ran is a small G protein that is essential for the translocation of RNA and proteins through the nuclear pore complex. The Ran protein has also been implicated in the control of DNA synthesis and cell cycle progression, as mutations in Ran have been found to disrupt DNA synthesis. Function Ran cycle Ran exists in the cell in two nucleotide-bound forms: GDP-bound and GTP-bound. RanGDP is converted into RanGTP through the action of RCC1, the nucleotide exchange factor for Ran. RCC1 is also known as RanGEF (Ran Guanine nucleotide Exchange Factor). Ran's intrinsic GTPase-activity is activated through interaction with Ran GTPase activating protein (RanGAP), facilitat ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
WPP Domain
The WPP domain is a protein domain thought to be exclusively found in plants, first identified in 2000. The domain is about 90 amino acid residues long. The domain is known to direct RanGAP to the nuclear envelope. Non-RanGAP nuclear envelope proteins are also known to encode WPP domains, such as MFP1 attachment factor 1 (MAF1), WPP1{{cite journal , vauthors=Patel S, Rose A, Meulia T, Dixit R, Cyr RJ, Meier I , title=Arabidopsis WPP-domain proteins are developmentally associated with the nuclear envelope and promote cell division , journal=The Plant Cell , volume=16 , issue=12 , pages=3260–73 , date=December 2004 , pmid=15548735 , pmc=535872 , doi=10.1105/tpc.104.026740 and WPP2. The WPP stands for a tryptophan-proline-proline motif that is highly conserved in the domain. Either deletion of the WPP domain or mutation of both the namesake tryptophan and first proline residues into alanine Alanine (symbol Ala or A), or α-alanine, is an α-amino acid that is used in the biosynt ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
RANBP2
RAN binding protein 2 (RANBP2) is protein which in humans is encoded by the ''RANBP2'' gene. It is also known as nucleoporin 358 (Nup358) since it is a member nucleoporin family that makes up the nuclear pore complex. RanBP2 has a mass of 358 kDa. Function RAN is a small GTP-binding protein of the RAS superfamily. Ran GTPase is a master regulatory switch, which among other functions, controls the shuttling of proteins between the nuclear and cytoplasm compartments of the cell. Ran GTPase controls a variety of cellular functions through its interactions with other proteins. The ''RanBP2'' gene encodes a very large RAN-binding protein that localizes to cytoplasmic filaments emanating from the nuclear pore complex. RanBP2/Nup358 is a giant scaffold and mosaic cyclophilin-related nucleoporin implicated in controlling selective processes of the Ran-GTPase cycle. RanBP2 is composed of multiple domains. Each domain of RanBP2 selectively and directly interacts with distinct proteins suc ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclear Envelope
The nuclear envelope, also known as the nuclear membrane, is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus, which encloses the genetic material. The nuclear envelope consists of two lipid bilayer membranes: an inner nuclear membrane and an outer nuclear membrane. The space between the membranes is called the perinuclear space. It is usually about 10–50 nm wide. The outer nuclear membrane is continuous with the endoplasmic reticulum membrane. The nuclear envelope has many nuclear pores that allow materials to move between the cytosol and the nucleus. Intermediate filament proteins called lamins form a structure called the nuclear lamina on the inner aspect of the inner nuclear membrane and give structural support to the nucleus. Structure The nuclear envelope is made up of two lipid bilayer membranes, an inner nuclear membrane and an outer nuclear membrane. These membranes are connected to each other by nuclear pores. Two sets of in ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Eukaryotes
Eukaryotes () are organisms whose cells have a nucleus. All animals, plants, fungi, and many unicellular organisms, are Eukaryotes. They belong to the group of organisms Eukaryota or Eukarya, which is one of the three domains of life. Bacteria and Archaea (both prokaryotes) make up the other two domains. The eukaryotes are usually now regarded as having emerged in the Archaea or as a sister of the Asgard archaea. This implies that there are only two domains of life, Bacteria and Archaea, with eukaryotes incorporated among archaea. Eukaryotes represent a small minority of the number of organisms, but, due to their generally much larger size, their collective global biomass is estimated to be about equal to that of prokaryotes. Eukaryotes emerged approximately 2.3–1.8 billion years ago, during the Proterozoic eon, likely as flagellated phagotrophs. Their name comes from the Greek εὖ (''eu'', "well" or "good") and κάρυον (''karyon'', "nut" or "kernel"). Eu ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nuclear Pore
A nuclear pore is a part of a large complex of proteins, known as a nuclear pore complex that spans the nuclear envelope, which is the double membrane surrounding the eukaryotic cell nucleus. There are approximately 1,000 nuclear pore complexes (NPCs) in the nuclear envelope of a vertebrate cell, but this number varies depending on cell type and the stage in the life cycle. The human nuclear pore complex (hNPC) is a 110 megadalton (MDa) structure. The proteins that make up the nuclear pore complex are known as nucleoporins; each NPC contains at least 456 individual protein molecules and is composed of 34 distinct nucleoporin proteins. About half of the nucleoporins typically contain solenoid protein domains—either an alpha solenoid or a beta-propeller fold, or in some cases both as separate structural domains. The other half show structural characteristics typical of "natively unfolded" or intrinsically disordered proteins, i.e. they are highly flexible proteins that lack ord ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Proceedings Of The National Academy Of Sciences Of The United States Of America
''Proceedings of the National Academy of Sciences of the United States of America'' (often abbreviated ''PNAS'' or ''PNAS USA'') is a peer-reviewed multidisciplinary scientific journal. It is the official journal of the National Academy of Sciences, published since 1915, and publishes original research, scientific reviews, commentaries, and letters. According to ''Journal Citation Reports'', the journal has a 2021 impact factor of 12.779. ''PNAS'' is the second most cited scientific journal, with more than 1.9 million cumulative citations from 2008 to 2018. In the mass media, ''PNAS'' has been described variously as "prestigious", "sedate", "renowned" and "high impact". ''PNAS'' is a delayed open access journal, with an embargo period of six months that can be bypassed for an author fee ( hybrid open access). Since September 2017, open access articles are published under a Creative Commons license. Since January 2019, ''PNAS'' has been online-only, although print issues are ava ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Protein Domain
In molecular biology, a protein domain is a region of a protein's polypeptide chain that is self-stabilizing and that folds independently from the rest. Each domain forms a compact folded three-dimensional structure. Many proteins consist of several domains, and a domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. In general, domains vary in length from between about 50 amino acids up to 250 amino acids in length. The shortest domains, such as zinc fingers, are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins. Background The concept of the domain was first proposed in 1973 by Wetlaufer aft ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
The Journal Of Cell Biology
The ''Journal of Cell Biology'' is a peer-reviewed scientific journal published by Rockefeller University Press. History In the early 1950s, a small group of biologists began to explore intracellular anatomy using the emerging technology of electron microscopy. Many of these researchers were at The Rockefeller Institute of Medicine, the predecessor of The Rockefeller University. As their work progressed to publication, they were disappointed with the limited quality of halftone image reproduction in the printed journals of the time, and frustrated by the narrow editorial policies of existing journals regarding their image-based results. In 1954, the Director of the Rockefeller Institute, Detlev Bronk, convened a luncheon to discuss the creation of a new journal as a venue for publication of this type of work. The first issue of ''The Journal of Biophysical and Biochemical Cytology'' was published less than a year later on January 25, 1955. A subscription cost $15 per year. The l ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
