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Study found that Pldn is present at presynaptic terminals, where it localizes to synaptic microtubules and the cytoskeleton; while pallidin does not have major roles in synaptic growth, structure, or function under basal conditions, pallidin is crucial to maintain the releasable synaptic vesicle pool during conditions of high activity. Stability of Pldn depends crucially on the BLOC-1 subunits dysbindin (show DTNBP1 Proteins) and blos1 (show BLOC1S1 Proteins).
Mecp2 regulates the expression of components belonging to the dysbindin (show DTNBP1 Proteins) interactome
no defects in the known components of pallidin-muted complex (BLOC-1)have been identif (show MUTED Proteins)ied in 142 patie (show BLOC1S1 Proteins)nts with HPS, suggesting that BLOC-1 function may be critical in humans.
Polycystin-2 (show PKD2 Proteins) requires IFT20 (show IFT20 Proteins)-GMAP210, the exocyst, and BLOC-1 for trafficking from endosomes to primary cilia.
We found 491 proteins sensitive to dysbindin (show DTNBP1 Proteins) and BLOC-1 loss of function
VAMP7 mediates fusion of BLOC-1-dependent transport carriers with melanosomes, illuminate SNARE recycling from melanosomes as a critical BLOC-3-dependent step.
Data suggest functional links between OCA2 and the BLOC-1, BLOC-2, and AP-3 protein complexes involved in melanosome biogenesis.
The identification of the feeble mutation led to our subsequent observations that AP-3 (show AP3B1 Proteins), as well as the BLOC-1 and BLOC-2 (show HPS6 Proteins) are essential for plasmacytoid dendritic cells signaling through TLR7 (show TLR7 Proteins) and TLR9 (show TLR9 Proteins).
This study demonstrated that Loss-of-function alleles of BLOC-1, Pldn(pa/pa), and Muted (show MUTED Proteins)(mu/mu) revealed that this complex acts as a brain-region-specific regulator of AP-3 (show AP3B1 Proteins).
pallidin may play a role in membrane fusion events required for melanosome biogenesis
BLOC-1, a novel complex containing this and muted (show MUTED Proteins) proteins involved in the biogenesis of melanosomes and platelet-dense granules
a Cappuccino frameshift mutation abolishes its ability to interact with pallidin-muted (show MUTED Proteins) complex (BLOC-1)in mice
The protein encoded by this gene may play a role in intracellular vesicle trafficking. It interacts with Syntaxin 13 which mediates intracellular membrane fusion. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined.
, BLOC-1 subunit 6
, biogenesis of lysosomal organelles complex-1, subunit 5, pallidin
, biogenesis of lysosome-related organelles complex 1 subunit 6
, pallid protein homolog
, syntaxin 13 binding protein 1
, syntaxin 13-interacting protein pallid
, pallidin homolog
, pallid protein
, syntaxin 13-interacting protein pallidin