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Gewählte Publikation:

Schoberer, J; Vavra, U; Stadlmann, J; Hawes, C; Mach, L; Steinkellner, H; Strasser, R.
(2009): Arginine/lysine residues in the cytoplasmic tail promote ER export of plant glycosylation enzymes.
Traffic. 2009; 10(1):101-115 FullText FullText_BOKU

Plant N-glycan processing enzymes are arranged along the early secretory pathway, forming an assembly line to facilitate the step-by-step modification of oligosaccharides on glycoproteins. Thus, these enzymes provide excellent tools to study signals and mechanisms, promoting their localization and retention in the endoplasmic reticulum (ER) and Golgi apparatus. Herein, we focused on a detailed investigation of amino acid sequence motifs present in their short cytoplasmic tails in respect to ER export. Using site-directed mutagenesis, we determined that single arginine/lysine residues within the cytoplasmic tail are sufficient to promote rapid Golgi targeting of Golgi-resident N-acetylglucosaminyltransferase I (GnTI) and alpha-mannosidase II (GMII). Furthermore, we reveal that an intact ER export motif is essential for proper in vivo function of GnTI. Coexpression studies with Sar1p provided evidence for COPII-dependent transport of GnTI to the Golgi. Our data provide evidence that efficient ER export of Golgi-resident plant N-glycan processing enzymes occurs through a selective mechanism based on recognition of single basic amino acids present in their cytoplasmic tails.
Autor*innen der BOKU Wien:
Mach Lukas
Schoberer Jennifer
Stadlmann Johannes
Steinkellner Herta
Strasser Richard
Vavra Ulrike
Find related publications in this database (using NML MeSH Indexing)
Amino Acid Sequence -
Arginine - genetics
Cytoplasm - enzymology
Endoplasmic Reticulum - enzymology
Glycosylation -
Golgi Apparatus - enzymology
Lysine - genetics
Mannosidases - chemistry
Molecular Sequence Data -
N-Acetylglucosaminyltransferases - chemistry
Protein Transport -
Recombinant Proteins - genetics
Spectrometry, Mass, Electrospray Ionization -
Tobacco - enzymology

Find related publications in this database (Keywords)
cytoplasmic tail
ER exit
Golgi targeting

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