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A family of proteins that stabilize the Ran/TC4 GTPase in its GTP-bound conformation by K.M. Lounsbury; A.L. Beddow; I.G. Macara is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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RanpTC4, referred to here as Ranl, is a 25-kilodalton nuclear GTP-binding protein with an acidic C terminus that lacks any consensus prenylation sites. Here, we use a nitrocellulose overlay assay to identify potential effector proteins that bind specifically and with high affinity to the GTP-bound form of Ranl. GTP-Ran1 is shown to bind a variety of proteins, present in many eukaryotic tissues and cell extracts. A 28-kDa protein is cytosolic, whereas others, consisting of proteins of 86-300 kDa, are primarily localized in the nucleus. Binding is highly specific and is not detected by other small GTPases, such as c-Ha-Ras or Rab3A. Both deletion of the C-terminal -DEDDDL acidic sequence or alteration of the N terminus of Ranl inhibits binding. However, these altered forms of Ranl maintain the capacity to bind guanyl nucleotides and interact with the nucleotide exchange factor. The Ranl-binding proteins potently inhibit release of GTP from Ranl. These proteins can therefore maintain Ranl in the "on" state and are potential downstream effectors for Rad-dependent cellular processes. Ranl' was initially identified as the gene product of TC4, an open reading frame cloned from a human ter

Who reads A family of proteins that stabilize the Ran/TC4 GTPase in its GTP-bound conformation?

Author

K.M. Lounsbury; A.L. Beddow; I.G. Macara

Publisher

Elsevier BV

Published

1994

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)