Partitioning to ordered membrane domains regulates the kinetics of secretory traffic
elifesciences.org
we find that Golgi exit kinetics are highly dependent on raft affinity, with raft preferring probes exiting Golgi ∼2.5-fold faster than probes with minimal raft affinity. We rationalize these observations with a kinetic model of secretory trafficking, wherein Golgi export can be facilitated by prote
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- we find that Golgi exit kinetics are highly dependent on raft affinity, with raft preferring probes exiting Golgi ∼2.5-fold faster than probes with minimal raft affinity. We rationalize these observations with a kinetic model of secretory trafficking, wherein Golgi export can be facilitated by protein association with raft domains. These observatio...
- afts have also been implicated in endocytic sorting (Gagescu et al., 2000), with some proteins relying on raft affinity for recycling to the PM after endocytosis (Diaz-Rohrer et al., 2023; Diaz-Rohrer et al., 2014b
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