Cycling of Q-linked B-N-acetylglucosamine on nucleocytoplasmic proteins  

Oleh:

Hart, Gerald W. ; Housley, Michael P ; Slawson, Chad

Jenis: Article from Journal - ilmiah internasional
Dalam koleksi: NATURE (keterangan: ada di Proquest) vol. 446 no. 7139 (Apr. 2007), page 1017.
Topik: Glycochemistry dan Glycobiology

Ketersediaan

Perpustakaan FK Nomor Panggil: N01.K.2007.04 Non-tandon: 1 (dapat dipinjam: 0) Tandon: tidak ada

Lihat Detail Induk

Isi artikel

All animals and plants dynamically attach and remove O-linked ~-N-acetylglucosamine (O-GIcNAc) at serine and threonine residues on myriad nuclear and cytoplasmic proteins. O-GIcNAc cycling, which is tightly regulated by the concerted actions of two highly conserved enzymes, serves as a nutrient and stress sensor. On some proteins, O-GIcNAc competes directly with phosphate for serine/threonine residues. Glycosylation with O-GIcNAc modulates signalling, and influences protein expression, degradation and trafficking. Emerging data indicate that O-GIcNAc glycosylation has a role in the aetiology of diabetes and neurodegeneration

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