Abstract：
:Different sites of plasma membrane attachment may underlie functional differences between isoforms of Ras. Here we show that palmitoylation and farnesylation targets H-ras to lipid rafts and caveolae, but that the interaction of H-ras with these membrane subdomains is dynamic. GTP-loading redistributes H-ras from rafts into bulk plasma membrane by a mechanism that requires the adjacent hypervariable region of H-ras. Release of H-ras-GTP from rafts is necessary for efficient activation of Raf. By contrast, K-ras is located outside rafts irrespective of bound nucleotide. Our studies identify a novel protein determinant that is required for H-ras function, and show that the GTP/GDP state of H-ras determines its lateral segregation on the plasma membrane.
journal_name
Nat Cell Bioljournal_title
Nature cell biologyauthors
Prior IA,Harding A,Yan J,Sluimer J,Parton RG,Hancock JFdoi
10.1038/35070050keywords:
subject
Has Abstractpub_date
2001-04-01 00:00:00pages
368-75issue
4eissn
1465-7392issn
1476-4679pii
35070050journal_volume
3pub_type
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