In the early secretory pathway, the delivery of anterograde cargoes from the endoplasmic reticulum (ER) exit sites (ERES) to the Golgi apparatus is a multi-step transport process occurring via the ER-Golgi intermediate compartment (IC, also called ERGIC). While the role microtubules in ER-to-Golgi transport has been well established, how the actin cytoskeleton contributes to this process remains poorly understood. Here, we report that Arp2/3 inhibition affects the network of acetylated microtubules around the Golgi and induces the accumulation of unusually long RAB1/GM130-positive carriers around the centrosome. These long carriers are less prone to reach the Golgi apparatus, and arrival of anterograde cargoes to the Golgi is decreased upon...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The cytosolic coat-protein complex COP-I interacts with cytoplasmic 'retrieval' signals present in m...
Protein traffic moving from the endoplasmic reticulum (ER) to the Golgi complex in mammalian cells p...
Actin is involved in the organization of the Golgi complex and Golgi-to-ER protein transport in mamm...
Actin is involved in the organization of the Golgi complex and Golgi-to-ER protein transport in mamm...
We recently demonstrated that dynein and kinesin motors drive multiple aspects of endosomal function...
To ensure their homeostasis and sustain differentiated functions, cells continuously transport diver...
Vesicular transport of protein and lipid cargo from the endoplasmic reticulum (ER) to cis-Golgi comp...
The Golgi complex is the central sorting and processing station of the secretory or anterograde path...
Bidirectional vesicular transport between the endoplasmic reticulum (ER) and Golgi is mediated large...
Vesicular transport of protein and lipid cargo from the endoplasmic reticulum (ER) to cis-Golgi comp...
SummaryTransport carriers operating between early compartments in the mammalian secretory pathway ha...
Organelle morphology of the endomembrane system is critical for optimal organelle function. ADP ribo...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The cytosolic coat-protein complex COP-I interacts with cytoplasmic 'retrieval' signals present in m...
Protein traffic moving from the endoplasmic reticulum (ER) to the Golgi complex in mammalian cells p...
Actin is involved in the organization of the Golgi complex and Golgi-to-ER protein transport in mamm...
Actin is involved in the organization of the Golgi complex and Golgi-to-ER protein transport in mamm...
We recently demonstrated that dynein and kinesin motors drive multiple aspects of endosomal function...
To ensure their homeostasis and sustain differentiated functions, cells continuously transport diver...
Vesicular transport of protein and lipid cargo from the endoplasmic reticulum (ER) to cis-Golgi comp...
The Golgi complex is the central sorting and processing station of the secretory or anterograde path...
Bidirectional vesicular transport between the endoplasmic reticulum (ER) and Golgi is mediated large...
Vesicular transport of protein and lipid cargo from the endoplasmic reticulum (ER) to cis-Golgi comp...
SummaryTransport carriers operating between early compartments in the mammalian secretory pathway ha...
Organelle morphology of the endomembrane system is critical for optimal organelle function. ADP ribo...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The Golgi apparatus controls the formation of non-centrosomal microtubule arrays important for Golgi...
The cytosolic coat-protein complex COP-I interacts with cytoplasmic 'retrieval' signals present in m...