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Human Polyclonal PLDN Primary Antibody for ELISA, WB - ABIN249879
Kouloumenta, Mavroidis, Capetanaki: Proper perinuclear localization of the TRIM-like protein myospryn requires its binding partner desmin. in The Journal of biological chemistry 2007
Show all 2 Pubmed References
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 and blos1.
Results from a study on gene expression variability markers in early-stage human embryos shows that BLOC1S6 (PLDN) is a putative expression variability marker for the 3-day, 8-cell embryo stage.
PLDN is a direct target of RUNX1 and its dysregulation is a mechanism for platelet dense granule deficiency associated with RUNX1 haplodeficiency
Mecp2 regulates the expression of components belonging to the dysbindin interactome
role in biogenesis of lysosome-related organelles
no defects in the known components of pallidin-muted complex (BLOC-1)have been identified in 142 patients with HPS, suggesting that BLOC-1 function may be critical in humans.
Polycystin-2 requires IFT20-GMAP210, the exocyst, and BLOC-1 for trafficking from endosomes to primary cilia.
We found 491 proteins sensitive to dysbindin 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, as well as the BLOC-1 and BLOC-2 are essential for plasmacytoid dendritic cells signaling through TLR7 and TLR9.
This study demonstrated that Loss-of-function alleles of BLOC-1, Pldn(pa/pa), and Muted(mu/mu) revealed that this complex acts as a brain-region-specific regulator of AP-3.
pallidin may play a role in membrane fusion events required for melanosome biogenesis
BLOC-1, a novel complex containing this and muted proteins involved in the biogenesis of melanosomes and platelet-dense granules
a Cappuccino frameshift mutation abolishes its ability to interact with pallidin-muted complex (BLOC-1)in mice
The coat-color phenotype of young homozygous double-mutant mice deficient in subunits of BLOC-3 (HPS1) and BLOC-1 (pallidin) was indistinguishable from that of BLOC-1 single mutants.
palladin is expressed in podocytes and plays an important role in actin dynamics.
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