| 1999 |
AP1M1 (μ1A) is a subunit of the ubiquitously expressed AP-1A clathrin adaptor complex, which mediates protein sorting at the trans-Golgi network (TGN) and endosomes, distinct from the epithelial-specific AP-1B complex containing μ1B. |
Stable cell line expression, immunofluorescence, immunoelectron microscopy, functional rescue in LLC-PK1 cells |
Cell |
High |
10338135 10535737
|
| 2000 |
Targeted disruption of the mouse μ1A-adaptin gene causes embryonic lethality at day 13.5; μ1A-deficient cells lack AP-1 binding to the TGN, and mannose 6-phosphate receptors (MPR46 and MPR300) are rerouted to endosomes, establishing that AP-1/μ1A is required for retrograde endosome-to-TGN transport of MPR. |
Mouse knockout (targeted gene disruption), subcellular fractionation, immunofluorescence, receptor trafficking assays |
The EMBO journal |
High |
10811610
|
| 2001 |
AP-1A (μ1A) and AP-1B (μ1B) localize to distinct subdomains of the TGN; only AP-1A colocalizes with furin, while AP-1B is found near recycling endosomes. AP-1B (but not AP-1A) expression also recruits exocyst subunits Sec8 and Exo70 required for basolateral transport. |
Immunofluorescence, immunoelectron microscopy, cell fractionation, epitope-tagged subunit expression |
The Journal of cell biology |
High |
11157985 14581457
|
| 2001 |
In μ1A-deficient fibroblasts, MPR300 endocytosis is enhanced seven-fold due to an increased internalization rate, with more MPR300 concentrated in clathrin-coated pits at the plasma membrane, demonstrating that AP-1/μ1A-mediated TGN recycling indirectly controls MPR300 plasma membrane recycling rate. |
Receptor internalization kinetics assay, electron microscopy of coated pits, μ1A-knockout fibroblasts |
Journal of cell science |
High |
11792812
|
| 2007 |
The N-terminal domain of μ1A regulates AP-1 membrane-to-cytoplasm recycling; a chimeric AP-1* complex bearing the μ2 N-terminal domain in place of the μ1A N-terminal domain shows slowed recycling kinetics and missorts mannose 6-phosphate receptors. |
Chimeric protein construction (μ1A/μ2 chimeras), FRAP, receptor trafficking assays |
Traffic |
Medium |
17988225
|
| 2010 |
AP-1 μ1A interacts with the C-terminal region of kidney anion exchanger 1 (kAE1) via a YXXØ motif (Y904DEV907); siRNA knockdown of μ1A decreases membrane localization of kAE1 and increases intracellular accumulation. |
Yeast two-hybrid, co-immunoprecipitation, GST pulldown, YFP-based protein fragment complementation assay, colocalization, siRNA knockdown |
Biochemical and biophysical research communications |
High |
20833140
|
| 2012 |
AP-1/μ1A (AP-1A complex) mediates somatodendritic sorting of transmembrane receptors in rat hippocampal neurons by recognizing signals in cytosolic domains of cargo proteins; AP-1 with clathrin functions in the neuronal soma to exclude somatodendritic proteins from axonal transport carriers, and perturbation affects dendritic spine morphology and synapse number. |
Dominant-negative constructs, siRNA knockdown, live imaging, immunofluorescence in primary hippocampal neurons |
Neuron |
High |
22958822
|
| 2012 |
AP-1A (μ1A) and AP-1B (μ1B) both interact via their μ1 subunits with the canonical YxxΦ motif (Y318xxV321) of the coxsackie and adenovirus receptor (CAR); AP-1A mediates biosynthetic sorting of CAR while AP-1B mediates basolateral recycling. |
Mutagenesis of sorting motifs, knockdown of μ1A/μ1B, co-immunoprecipitation, polarized sorting assays in MDCK cells |
Proceedings of the National Academy of Sciences of the United States of America |
High |
22343291
|
| 2012 |
AP-1 μ1A (AP1M1) and γ2 subunit of AP-1 are required for Nef-mediated lysosomal targeting of CD4; depletion of μ1A or γ2 (but not γ1) causes CD4 to accumulate in early endosomes after Nef-induced internalization, preventing lysosomal degradation. |
siRNA knockdown, co-immunoprecipitation, flow cytometry, immunofluorescence |
Journal of cell science |
Medium |
27909244
|
| 2012 |
A noncanonical tripartite hydrophobic motif (Trp13/Val16/Met20) in the N terminus of HIV-1 Nef acts as a noncanonical μ1A-binding motif that interacts with the tyrosine motif-binding site of μ1A and is required for MHC-I downregulation in T lymphocytes. |
Mutagenesis, co-immunoprecipitation, flow cytometry, molecular docking |
Journal of virology |
Medium |
22301137
|
| 2012 |
AP-1A (μ1A) and AP-1B (μ1B) interact with kAE1 via reciprocal co-immunoprecipitation in epithelial cells and in vivo in mouse kidney; knockdown of endogenous μ1A prevents kAE1 trafficking to the plasma membrane and leads to its lysosomal degradation, establishing AP-1A as the primary regulator of basolateral kAE1 trafficking. |
Reciprocal co-immunoprecipitation, siRNA knockdown, immunofluorescence, cell surface biotinylation |
American journal of physiology. Cell physiology |
High |
22744004
|
| 2013 |
μ1A and μ1B isoforms of AP-1 largely colocalize at both TGN and recycling endosome membranes; they differ primarily in signal-recognition specificity, with μ1B preferentially binding a subset of basolateral sorting signals unrecognized by μ1A, expanding the repertoire of cargo sorted to the basolateral surface. |
Improved immunofluorescence colocalization, co-immunoprecipitation, in vitro binding assays with cargo peptides, siRNA knockdown |
Developmental cell |
High |
24229647
|
| 2013 |
μ1A associates with IRS-1 via three YXXØ motifs in IRS-1; AP-1-dependent transport is required for IRS-1 localization to peripheral vesicles, and deletion of these AP-1 binding sites impairs IGF-I-induced cell proliferation and reduces IRS-1 tyrosine phosphorylation and PI3-kinase association. |
Co-immunoprecipitation, YXXØ motif mutagenesis, siRNA knockdown, subcellular fractionation, proliferation assays |
Molecular and cellular biology |
Medium |
23478262
|
| 2013 |
PREPL (a cytoplasmic prolyl-oligopeptidase-like protein) interacts with the N-terminal 70 amino acids of μ1A via yeast two-hybrid; PREPL overexpression reduces AP-1 membrane binding while reduced PREPL expression increases membrane binding and impairs AP-1 recycling, identifying PREPL as a regulator of AP-1 membrane-cytoplasm recycling. |
Yeast two-hybrid, PREPL overexpression/knockdown, membrane fractionation, colocalization by immunofluorescence |
Journal of cell science |
Medium |
23321636
|
| 2014 |
AP-1A (μ1A subunit) is required for secretory granule (SG) biogenesis in neuroendocrine cells; reduced μ1A levels cause loss of TGN cisternae and immature SGs, missorting of carboxypeptidase D (CPD) and PAM-1 into non-condensing granules, and impaired stimulated peptide secretion. Yeast two-hybrid demonstrated direct interaction of μ1A with the PAM-1 cytosolic domain. |
shRNA knockdown, metabolic labeling, secretion assays, immunofluorescence, yeast two-hybrid, co-immunoprecipitation |
Traffic |
Medium |
25040637
|
| 2014 |
AP-1A (μ1A) and AP-1B (μ1B) together mediate basolateral sorting of the Mg2+ transporter CNNM4; simultaneous knockdown of both μ1A and μ1B abrogates basolateral localization, and three conserved dileucine motifs in CNNM4 are required for interaction with both μ1A and μ1B. |
siRNA knockdown (single and double), mutagenesis of dileucine motifs, co-immunoprecipitation, immunofluorescence in MDCK cells |
Biochemical and biophysical research communications |
Medium |
25449265
|
| 2015 |
Reduced AP-1/μ1A function alters endocytic trafficking of PAM (peptidylglycine α-amidating monooxygenase), causing PAM-1 accumulation on the cell surface and impairing copper-dependent amidation activity; co-immunoprecipitation supports that PAM and Atp7a occupy the same subcellular compartment via AP-1-dependent trafficking. |
shRNA knockdown, cell surface biotinylation, co-immunoprecipitation, copper chelation assays, immunofluorescence |
The Journal of biological chemistry |
Medium |
26170456
|
| 2017 |
The C-terminal domain of μ1A (AP1M1) binds the cytoplasmic tail of L-selectin via a novel basic binding motif (cluster of dibasic residues 356RR357, 359KK360, 362KK363 and 369DD370); L-selectin colocalizes with AP-1 at the TGN and phosphorylation of the L-selectin tail blocks this interaction, suggesting AP-1/μ1A mediates constitutive retrograde transport of L-selectin to a TGN reserve pool. |
Peptide pulldown combined with LC-MS, GST pulldown domain mapping, co-immunoprecipitation, mutagenesis, molecular docking, immunofluorescence colocalization |
The Journal of biological chemistry |
Medium |
28235798
|
| 2018 |
VZV tegument protein ORF9p interacts with AP1M1 (μ1 subunit of AP-1); a leucine-231-containing dileucine motif in ORF9p is critical for this interaction, and mutation of this leucine impairs viral growth by preventing efficient secondary envelopment of the virus. |
Yeast two-hybrid, co-immunoprecipitation in infected cells, site-directed mutagenesis, viral growth assays |
Journal of virology |
Medium |
29793951
|
| 2025 |
AP1M1 knockout identified in an unbiased CRISPR/Cas9 screen as a modifier of antisense oligonucleotide (ASO) activity; AP1M1 absence strongly increases ASO activity by delaying endosome-to-lysosome transport both in vitro and in vivo, prolonging ASO residence in the endosomal system and increasing endosomal escape. |
CRISPR/Cas9 knockout screen, genetic splice reporter, endosome-to-lysosome transport assays in vitro and in vivo |
Nature communications |
High |
40588516
|
| 1995 |
The N-terminal region (approximately amino acids 130–350) of γ-adaptin determines AP-1 complex targeting and co-assembly with AP47 (μ1A) and AP19 (σ1), as shown by chimeras and yeast two-hybrid interactions between γ-adaptin and AP47. |
Adaptin chimera construction, immunoprecipitation, yeast two-hybrid |
The Journal of cell biology |
Medium |
7593184
|
| 1994 |
The C. elegans unc-101 gene encodes a homolog of AP47 (μ1A); mouse AP47 and UNC-101 are functionally equivalent in transgenic nematodes, demonstrating conservation of clathrin-associated medium chain function. UNC-101 is required for negative regulation of vulval differentiation and multiple developmental processes. |
Genetic epistasis, transgenic rescue in C. elegans, sequence analysis |
Genes & development |
Medium |
8288128
|
| 2014 |
AP-1 μ1A, AP-3 μ1, and AP-4 μ1 (but not AP-1 μ1B, PKD1, or PKD2) are required for intracellular sorting and trafficking of kAE1 from TGN to the basolateral membrane; AP-1 μ1A co-localizes with kAE1 in human kidney tissue. |
siRNA knockdown, co-immunoprecipitation, YFP-based protein fragment complementation assay, immunofluorescence on human kidney tissue |
Traffic |
Medium |
24698155
|