title: Golgi-to-plastid trafficking of proteins through secretory pathway: Insights into vesicle-mediated import toward the plastids.
abstract: The diversity of protein targeting pathways to plastids and their regulation in response to developmental and metabolic status is a key issue in the regulation of cellular function in plants. The general import pathways that target proteins into and across the plastid envelope with changes in gene expression are critical for plant development by regulating the response to physiological and metabolic changes within the cell. Glycoprotein targeting to complex plastids involves routing through the secretory pathway, among others. However, the mechanisms of trafficking via this system remain poorly understood. The present article discusses our results in site-specific N-glycosylation of nucleotide pyrophosphatase/phosphodiesterases (NPPs) glycoproteins and highlights protein delivery in Golgi/plastid pathway via the secretory pathway. Furthermore, we outline the hypotheses that explain the mechanism for importing vesicles trafficking with nucleus-encoded proteins into plastids.
authors.affiliation: a Department of Applied Biological Chemistry , Faculty of Agriculture, Niigata University , Niigata , Japan.|b Graduate School of Science and Technology , Niigata University , Ikarashi, Niigata , Japan.
authors.forename: Marouane
authors.initials: M
authors.lastname: Baslam
authors.affiliation: a Department of Applied Biological Chemistry , Faculty of Agriculture, Niigata University , Niigata , Japan.
authors.forename: Kazusato
authors.initials: K
authors.lastname: Oikawa
authors.affiliation: a Department of Applied Biological Chemistry , Faculty of Agriculture, Niigata University , Niigata , Japan.
authors.forename: Aya
authors.initials: A
authors.lastname: Kitajima-Koga
authors.affiliation: b Graduate School of Science and Technology , Niigata University , Ikarashi, Niigata , Japan.
authors.forename: Kentaro
authors.initials: K
authors.lastname: Kaneko
authors.affiliation: a Department of Applied Biological Chemistry , Faculty of Agriculture, Niigata University , Niigata , Japan.|b Graduate School of Science and Technology , Niigata University , Ikarashi, Niigata , Japan.
authors.forename: Toshiaki
authors.initials: T
authors.lastname: Mitsui
mesh_terms: D002467:Cell Nucleus / Q000378:metabolism; D006023:Glycoproteins / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism*; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism; D018087:Plastids / Q000378:metabolism*; D021381:Protein Transport; D011755:Pyrophosphatases / Q000378:metabolism; D055571:Secretory Pathway / Q000502:physiology
chemical_list: D006023:Glycoproteins; D010727:Phosphoric Diester Hydrolases; D011755:Pyrophosphatases; C021899:nucleotide pyrophosphatase
keywords: Glycoprotein; N-glycoproteomes; golgi-vesicle budding; invagination; nucleotide pyrophosphatase/phosphodiesterases; pass-through model; signal peptide; trans-Golgi compartments; vesicle-mediated pathway