Selected article for: "appropriate compartment and ER protein"

Author: Maceyka, Michael; Machamer, Carolyn E.
Title: Ceramide Accumulation Uncovers a Cycling Pathway for the cis-Golgi Network Marker, Infectious Bronchitis Virus M Protein
  • Document date: 1997_12_15
  • ID: wekvet6f_2
    Snippet: T he organelles of the classical secretory pathway must maintain their identity despite a large flux of lipids and proteins. Two models have emerged to explain how proteins can be maintained in specific compartments (Machamer, 1993; Nilsson and Warren, 1994 ). The retention model proposes that proteins are efficiently anchored in the appropriate compartment. The retrieval model proposes that proteins are continually recycled from later compartmen.....
    Document: T he organelles of the classical secretory pathway must maintain their identity despite a large flux of lipids and proteins. Two models have emerged to explain how proteins can be maintained in specific compartments (Machamer, 1993; Nilsson and Warren, 1994 ). The retention model proposes that proteins are efficiently anchored in the appropriate compartment. The retrieval model proposes that proteins are continually recycled from later compartments. The two models are not mutually exclusive; indeed most proteins within the secretory pathway probably use both mechanisms for localization, albeit to differing extents. An example of this is the localization of the ER resident protein BiP, which contains a KDEL retrieval signal but is only slowly secreted when this signal is removed (Munro and Pelham, 1987) . This suggests that other parts of the molecule may contain retention information.

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