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

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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).[1] Plant RanGAP proteins do not contain the protein domain necessary for association with Nup358 but are targeted to the nuclear rim by the plant-specific WPP domain.[2] In contrast to plant and animal cells, yeast RanGAP is located in the cytosol.[3]

RanGAP and the origin of eukaryotes

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Together with RCC1 and components of the nuclear pore, RanGAP has been suggested to have evolved at the origin of eukaryotes.[4]

References

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  1. ^ Matunis MJ, Wu J, Blobel G (February 1998). "SUMO-1 modification and its role in targeting the Ran GTPase-activating protein, RanGAP1, to the nuclear pore complex". The Journal of Cell Biology. 140 (3): 499–509. doi:10.1083/jcb.140.3.499. PMC 2140169. PMID 9456312.
  2. ^ Rose A, Meier I (December 2001). "A domain unique to plant RanGAP is responsible for its targeting to the plant nuclear rim". Proceedings of the National Academy of Sciences of the United States of America. 98 (26): 15377–82. Bibcode:2001PNAS...9815377R. doi:10.1073/pnas.261459698. PMC 65037. PMID 11752475.
  3. ^ Hopper AK, Traglia HM, Dunst RW (August 1990). "The yeast RNA1 gene product necessary for RNA processing is located in the cytosol and apparently excluded from the nucleus". The Journal of Cell Biology. 111 (2): 309–21. doi:10.1083/jcb.111.2.309. PMC 2116204. PMID 2116418.
  4. ^ Cavalier-Smith T (2010). "Origin of the cell nucleus, mitosis and sex: roles of intracellular coevolution". Biology Direct. 5: 7. doi:10.1186/1745-6150-5-7. PMC 2837639. PMID 20132544.

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WPP domain

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

Ran (protein)

GTPase-activity is activated through interaction with Ran GTPase activating protein (RanGAP), facilitated by complex formation with Ran-binding protein (RanBP). GTPase-activation

RANBP1

Characterization of the Ran-RanBP1-RanGAP System: Are RanBP Proteins and the Acidic Tail of RanGAP Required for the Ran-RanGAP GTPase Reaction?". Mol. Cell

Intragenomic conflict

main drive locus, a truncated tandem duplication of the gene RanGAP on chromosome 2L (Sd-RanGAP) targets a repetitive array of satellite DNA on chromosome

XPO5

transporting pre-miRNA into the cytoplasm in the process. Once in the cytoplasm, RanGAP hydrolyzes GTP to GDP, causing a conformational change that releases the

LRRC73

Description E-value 444072 28..254 COG5238, RNA1, Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure

Importin

still bound to Ran-GTP. Once in the cytoplasm, Ran-GTP is hydrolysed by RanGAP, forming Ran-GDP, and releasing the two importins for further activity.

RANBP2

SP100. Another target for SUMOylation is RanGAP which is the GTPase activating protein for Ran. SUMO-RanGAP interacts with a domain near the carboxyl