GRASP65 and GRASP55 sequentially promote the transport of C-terminal valine-bearing cargos to and through the Golgi complex.
about
An OBSL1-Cul7Fbxw8 ubiquitin ligase signaling mechanism regulates Golgi morphology and dendrite patterningGolgi reassembly stacking protein 55 interacts with membrane-type (MT) 1-matrix metalloprotease (MMP) and furin and plays a role in the activation of the MT1-MMP zymogenGRASPs in Golgi Structure and FunctionATP2C1 gene mutations in Hailey-Hailey disease and possible roles of SPCA1 isoforms in membrane traffickingThe yeast GRASP Grh1 colocalizes with COPII and is dispensable for organizing the secretory pathway.Caspase cleavage of the Golgi stacking factor GRASP65 is required for Fas/CD95-mediated apoptosis.GRASP55 and GRASP65 play complementary and essential roles in Golgi cisternal stackingGenetic, structural, and chemical insights into the dual function of GRASP55 in germ cell Golgi remodeling and JAM-C polarized localization during spermatogenesis.Dual anchoring of the GRASP membrane tether promotes trans pairingNew components of the Golgi matrix.Mitotic inhibition of GRASP65 organelle tethering involves Polo-like kinase 1 (PLK1) phosphorylation proximate to an internal PDZ ligandThe golgin coiled-coil proteins of the Golgi apparatus.The B7-1 cytoplasmic tail enhances intracellular transport and mammalian cell surface display of chimeric proteins in the absence of a linear ER export motif.The role of GRASP65 in Golgi cisternal stacking and cell cycle progression.Sequential phosphorylation of GRASP65 during mitotic Golgi disassembly.Regulation of protein glycosylation and sorting by the Golgi matrix proteins GRASP55/65.The many routes of Golgi-dependent trafficking.A positive signal prevents secretory membrane cargo from recycling between the Golgi and the ER.Sedlin controls the ER export of procollagen by regulating the Sar1 cycle.Golgi structure formation, function, and post-translational modifications in mammalian cells.TGFB1 is secreted through an unconventional pathway dependent on the autophagic machinery and cytoskeletal regulators.Knockout of the Golgi stacking proteins GRASP55 and GRASP65 impairs Golgi structure and function.Mitotic inheritance of the Golgi complex and its role in cell division.Synchronization of secretory protein traffic in populations of cells.Structural Basis for the Interaction between Golgi Reassembly-stacking Protein GRASP55 and Golgin45.The unconventional secretion of ARMS2.Subclass-specific localization and trafficking of Arabidopsis p24 proteins in the ER-Golgi interface.Monomerization and ER Relocalization of GRASP Is a Requisite for Unconventional Secretion of CFTR.
P2860
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P2860
GRASP65 and GRASP55 sequentially promote the transport of C-terminal valine-bearing cargos to and through the Golgi complex.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@en
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@nl
type
label
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@en
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@nl
prefLabel
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@en
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@nl
P2093
P2860
P50
P356
P1476
GRASP65 and GRASP55 sequential ...... and through the Golgi complex.
@en
P2093
Galina Beznoussenko
Gianluca Martire
Giuseppe Di Tullio
Libera Prencipe
Luisa Iodice
Pierfrancesco Marra
Stefano Bonatti
P2860
P304
34849-34860
P356
10.1074/JBC.M109.068403
P407
P577
2009-10-19T00:00:00Z