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10.1074/jbc.M114.568311

http://scihub22266oqcxt.onion/10.1074/jbc.M114.568311
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C4059126!4059126 !24778190
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suck abstract from ncbi


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pmid24778190
      J+Biol+Chem 2014 ; 289 (24 ): 16835-43
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  • The ?-helical region in p24?2 subunit of p24 protein cargo receptor is pivotal for the recognition and transport of glycosylphosphatidylinositol-anchored proteins #MMPMID24778190
  • Theiler R ; Fujita M ; Nagae M ; Yamaguchi Y ; Maeda Y ; Kinoshita T
  • J Biol Chem 2014[Jun]; 289 (24 ): 16835-43 PMID24778190 show ga
  • Glycosylphosphatidylinositol-anchored proteins (GPI-APs) are group of proteins that depend on p24 cargo receptors for their transport from the endoplasmic reticulum to the Golgi apparatus. The GPI anchor is expected to act as a sorting and transport signal, but so far little is known about the recognition mechanism. In the present study we investigate the GPI-AP transport in cell knockdown of p24?, the most diverse p24 subfamily. Knockdown of p24?2 but not of other p24? family members impaired the transport of a reporter GPI-AP. Restoration of the knockdown-induced phenotype using chimeric constructs between p24?2 and the related p24?1 further implied a role of the ?-helical region of p24?2 but not its GOLD domain in the specific binding of GPI-APs. We conclude that motifs in the membrane-adjacent ?-helical region of p24?2 are involved in recognition of GPI-APs and are consequently responsible for the incorporation of these proteins into coat protein complex II-coated transport vesicles.
  • |Amino Acid Motifs [MESH]
  • |Amino Acid Sequence [MESH]
  • |Animals [MESH]
  • |Binding Sites [MESH]
  • |CHO Cells [MESH]
  • |Calcium Channels [MESH]
  • |Cricetinae [MESH]
  • |Cricetulus [MESH]
  • |GPI-Linked Proteins/*metabolism [MESH]
  • |Humans [MESH]
  • |Mice [MESH]
  • |Molecular Sequence Data [MESH]
  • |Protein Binding [MESH]
  • |Protein Subunits/chemistry/genetics/metabolism [MESH]
  • |Protein Transport [MESH]
  • |TRPV Cation Channels [MESH]


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