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The role of MyRIP in Ca(2+)-driven exocytosis requires both MyoVa- and actin-binding potential.
Myrip couples the retention of secretory granules in the cell cortex, their transport to the plasma membrane, and their attachment to the plasma membrane, thus promoting secretion.
A Rab27a (show RAB27A Proteins)/MyRIP/myosin Va (show MYO5A Proteins) complex is involved in linking von-Willebrand factor (Vwf (show VWF Proteins)) to the peripheral actin cytoskeleton of endothelial cells to allow full maturation and prevent premature secretion of vWF (show VWF Proteins).
A new potentially protective effect was identified at rs2679798 in MYRIP.
a molecular complex composed of Rab27A, MyRIP and myosin VIIa bridges retinal melanosomes to the actin cytoskeleton and thereby mediates the local trafficking of these organelles
Slac2c/MyRIP is part of a complex mediating the interaction of secretory granules with cortical actin cytoskeleton
During primate spermiogenesis, dynein, myosin Va, MyRIP and Rab27b that compose microtubule-based and actin-based vesicle transport systems are actually present in the manchette and might possibly be involved in intramanchette transport.
Rab27a (show RAB27A Proteins) and MyRIP regulate the amount and multimeric state of VWF (show VWF Proteins) released from endothelial cells.
Slac2-c/MyRIP contains an N-terminal Slp (show SEPT9 Proteins) homology domain (SHD (show SHD Proteins)) and functions as a linker protein (show LAT Proteins) that interacts with myosin Rab27A/B (show RAB27A Proteins), VIIa/Va, and actin.
Exophilin8 transiently clusters insulin granules at the actin-rich cell cortex prior to exocytosis
Slac2-c acts as a functional myosin VIIa receptor and the Rab27A.Slac2-c x myosin VIIa tripartite protein complex regulates the transport of retinal melanosomes in pigment epithelium cells
The present results provide evidence from live retinal pigment epithelium cells that the RAB27A-MYRIP-MYO7A complex functions in melanosome motility.
Results suggest that the Rab27a-Myrip-MyoVIIa complex regulates tethering of melanosomes onto actin filaments, a process that ensures melanosome movement towards the cell periphery.
indicate that MyRIP functions as a scaffolding protein that links protein kinase A to components of the exocytosis machinery
Myrip is a versatile Rab27a-associated myosin-activating protein that mediates cellular activation of MyoVa and MyoVIIa via non-overlapping domains.
Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity).
Slp homologue lacking C2 domains
, myosin-VIIa- and Rab-interacting protein
, rab effector MyRIP
, slp homolog lacking C2 domains c
, synaptotagmin-like protein homologue lacking C2 domains-c
, synaptotagmin-like protein lacking C2 domains C
, exophilin 8
, myosin VIIA and Rab interacting protein
, A kinase-anchoring protein
, rab effector MyRIP-like