Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange.

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Standard

Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. / Soldati, Thierry; Shapiro, Allan D.; Svejstrup, AB; Pfeffer, SR.

I: Nature, 1994, s. 76-78.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Soldati, T, Shapiro, AD, Svejstrup, AB & Pfeffer, SR 1994, 'Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange.', Nature, s. 76-78. https://doi.org/10.1038/369076a0

APA

Soldati, T., Shapiro, A. D., Svejstrup, AB., & Pfeffer, SR. (1994). Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature, 76-78. https://doi.org/10.1038/369076a0

Vancouver

Soldati T, Shapiro AD, Svejstrup AB, Pfeffer SR. Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. Nature. 1994;76-78. https://doi.org/10.1038/369076a0

Author

Soldati, Thierry ; Shapiro, Allan D. ; Svejstrup, AB ; Pfeffer, SR. / Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange. I: Nature. 1994 ; s. 76-78.

Bibtex

@article{2800000fae8e451bbaedb650769d93e8,

title = "Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange.",

abstract = "The Rab GTPases are key regulators of vesicular transport. A fraction of Rab proteins is present in the cytosol, bound with GDP, complexed to a protein termed GDI. Rab9 is localized primarily to late endosomes, where it aids the transport of mannose 6-phosphate receptors to the trans-Golgi network. It has been proposed that Rab proteins are delivered to specific membranes by GDI, and that this process is accompanied by the exchange of bound GDP for GTP. In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants. Here we describe the reconstitution of the selective targeting of prenylated Rab9 protein onto late endosome membranes and show that this process is accompanied by endosome-triggered nucleotide exchange.",

author = "Thierry Soldati and Shapiro, {Allan D.} and AB Svejstrup and SR Pfeffer",

year = "1994",

doi = "10.1038/369076a0",

language = "English",

pages = "76--78",

journal = "Nature",

issn = "0028-0836",

publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - Membrane targeting of the small GTPase Rab9 is accompanied by nucleotide exchange.

AU - Soldati, Thierry

AU - Shapiro, Allan D.

AU - Svejstrup, AB

AU - Pfeffer, SR

PY - 1994

Y1 - 1994

N2 - The Rab GTPases are key regulators of vesicular transport. A fraction of Rab proteins is present in the cytosol, bound with GDP, complexed to a protein termed GDI. Rab9 is localized primarily to late endosomes, where it aids the transport of mannose 6-phosphate receptors to the trans-Golgi network. It has been proposed that Rab proteins are delivered to specific membranes by GDI, and that this process is accompanied by the exchange of bound GDP for GTP. In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants. Here we describe the reconstitution of the selective targeting of prenylated Rab9 protein onto late endosome membranes and show that this process is accompanied by endosome-triggered nucleotide exchange.

AB - The Rab GTPases are key regulators of vesicular transport. A fraction of Rab proteins is present in the cytosol, bound with GDP, complexed to a protein termed GDI. Rab9 is localized primarily to late endosomes, where it aids the transport of mannose 6-phosphate receptors to the trans-Golgi network. It has been proposed that Rab proteins are delivered to specific membranes by GDI, and that this process is accompanied by the exchange of bound GDP for GTP. In addition, Rab localization requires carboxy-terminal prenylation and specific structural determinants. Here we describe the reconstitution of the selective targeting of prenylated Rab9 protein onto late endosome membranes and show that this process is accompanied by endosome-triggered nucleotide exchange.

U2 - 10.1038/369076a0

DO - 10.1038/369076a0

M3 - Journal article

C2 - 8164745

SP - 76

EP - 78

JO - Nature

JF - Nature

SN - 0028-0836

ER -

ID: 334652972