| 1995 |
GM130 (GOLGA2) is a peripheral cytoplasmic protein tightly bound to Golgi membranes at the cis-Golgi network, forming part of a larger oligomeric complex. It has extended rod-like structure with coiled-coil domains and is not redistributed to the ER by brefeldin A treatment. |
Biochemical fractionation, immunofluorescence microscopy, immunoelectron microscopy, cDNA cloning |
The Journal of cell biology |
High |
8557739
|
| 1997 |
GM130 N-terminus directly binds the vesicle-docking protein p115, providing a membrane docking site for COPI vesicles at the cis-Golgi. Mitotic phosphorylation of GM130 prevents p115 binding, explaining Golgi fragmentation at mitosis onset. An N-terminal GM130 peptide inhibited NSF-dependent (but not p97-dependent) reassembly of Golgi cisternae from mitotic fragments. |
Deletion analysis, co-immunoprecipitation, in vitro Golgi reassembly assay, peptide inhibition |
Cell |
High |
9150144
|
| 1998 |
Cdc2 (CDK1) kinase directly phosphorylates GM130 at a single serine residue (Ser-25), and this phosphorylation is required for mitotic Golgi fragmentation. MEK1 was shown not to be required for GM130 phosphorylation or mitotic Golgi fragmentation either in vitro or in vivo. |
In vitro kinase assay, site-directed mutagenesis, mass spectrometry peptide mapping, cell-based fragmentation assay |
Cell |
High |
9753325
|
| 1998 |
GRASP65 and GM130 form a complex on Golgi membranes that can recruit p115. The GRASP65 binding site on GM130 maps to the sequence xxNDxxxIMVI-COOH at the C-terminus (also required for Golgi localization), and the GM130-binding site on GRASP65 maps to amino acids 189–201. GFP-reporter experiments showed that the GRASP65–GM130 interaction is required for correct targeting of both proteins to the Golgi. |
Gel filtration, immunoprecipitation, in vitro translation, site-directed mutagenesis, GFP fusion reporters |
The EMBO journal |
High |
9628863
|
| 2000 |
GM130 is phosphorylated on Ser-25 in prophase coinciding with Golgi breakdown; it remains phosphorylated through metaphase/anaphase and is dephosphorylated in telophase during Golgi reassembly. PP2A containing the Bα regulatory subunit was identified as the phosphatase responsible for dephosphorylating GM130 Ser-25 at mitotic exit. |
Phosphospecific antibody, temporal cell-cycle analysis, phosphatase inhibitor studies, immunoprecipitation of phosphatase |
The Journal of cell biology |
High |
10769027
|
| 2000 |
Inhibition of p115 binding to GM130 (by microinjection of N-terminal GM130 peptide or overexpression of N-terminal-deleted GM130) increases the number of COP-sized transport vesicles and significantly inhibits VSV-G protein intracellular transport, demonstrating that the GM130–p115 tethering complex increases efficiency of vesicle fusion with the Golgi. |
Microinjection, overexpression, immunofluorescence quantification, electron microscopy |
Molecular biology of the cell |
High |
10679020
|
| 2000 |
Anti-GM130 antibodies inhibit VSV-G transport to the mannosidase II-containing Golgi compartment at a step after the p115-requiring step but before the giantin-requiring step, indicating a sequential role for p115, GM130, and giantin in ER-to-Golgi trafficking. |
Antibody microinjection, VSV-G transport assay, immunofluorescence |
The Journal of biological chemistry |
Medium |
11035033
|
| 2001 |
GM130, complexed with GRASP65 and other proteins, forms a Rab1 effector complex that interacts with activated Rab1-GTP in a p115-independent manner, and is required for COPII vesicle targeting/fusion with the cis-Golgi. |
GST pulldown, co-immunoprecipitation, vesicle transport assay |
Traffic (Copenhagen, Denmark) |
Medium |
11285137
|
| 2001 |
Rab1b interacts specifically with GM130 in a GTP-dependent manner requiring the hypervariable N- and C-termini of Rab1b, with the Rab1b-binding site on GM130 distinct from the p115 and GRASP65 binding sites. |
Yeast two-hybrid screen, in vitro binding assay, mutagenesis |
EMBO reports |
Medium |
11306556
|
| 2001 |
GST-Rab33b (GTP-locked) interacts with GM130 by Western blotting/mass spectrometry, identifying GM130 as a putative effector of Rab33b, which regulates retrograde Golgi-to-ER transport. |
GST pulldown, mass spectrometry, microinjection of Rab33b mutants |
FEBS letters |
Low |
11718716
|
| 2004 |
GM130 acts as a scaffold to recruit mammalian Ste20 kinases YSK1 and MST4 to the Golgi apparatus, and GM130 binding activates these kinases by promoting autophosphorylation of a conserved T-loop threonine. YSK1 phosphorylates 14-3-3ζ as a substrate at the Golgi. Interference with YSK1 disrupts perinuclear Golgi organization, cell migration, and collagen invasion. |
Co-immunoprecipitation, in vitro kinase assay, dominant-negative expression, biochemical substrate screen |
The Journal of cell biology |
High |
15037601
|
| 2006 |
GM130 and GRASP65 are required for lateral cisternal fusion events that form the continuous Golgi ribbon, and these fusion events are necessary for uniform distribution of Golgi enzymes across the ribbon. |
siRNA knockdown, live-cell imaging, fluorescence recovery after photobleaching (FRAP), enzyme distribution assay |
Nature cell biology |
High |
16489344
|
| 2007 |
GM130 directly binds syntaxin 5 (a t-SNARE) via the membrane-proximal region of GM130. p115 binding to a distal site in GM130 inhibits GM130's interaction with syntaxin 5 and with Rab1. Mitotic phosphorylation also inhibits these interactions. GM130 depletion by RNAi slows ER-to-Golgi trafficking in vivo. |
Co-immunoprecipitation, in vitro binding assay, mutagenesis, RNAi knockdown, transport assay |
The Journal of biological chemistry |
High |
18167358
|
| 2007 |
GM130 depletion by RNAi in human cells causes abnormal interphase centrosomes that are mispositioned and defective for microtubule organization and cell migration; when depleted cells enter mitosis, they form multipolar spindles and arrest in metaphase. |
RNA interference (RNAi), immunofluorescence, live-cell imaging, cell migration assay |
Molecular biology of the cell |
Medium |
18045989
|
| 2007 |
GM130 cycling between cis-Golgi compartments and ER-to-Golgi carriers (EGCs) is required for homotypic tethering and fusion of EGCs and their incorporation into Golgi stacks to form the Golgi ribbon. In absence of GM130, EGCs remain as distinct entities causing tubulovesicular membrane accumulation, shortened cisternae, and ribbon breakdown. |
siRNA knockdown, electron microscopy, live-cell imaging, cargo trafficking assay |
Molecular biology of the cell |
Medium |
17314401
|
| 2008 |
GM130 regulates centrosome organization through a Golgi-associated complex with the Rho GEF Tuba and Cdc42. GM130 interaction with Tuba controls Tuba-mediated activation of Cdc42 at the Golgi; blocking Tuba or Cdc42 reproduces GM130-depletion centrosome phenotype; constitutively active Cdc42 bypasses the requirement for GM130 in centrosome regulation, placing Cdc42 downstream of GM130. |
Co-immunoprecipitation, RNAi knockdown, constitutively active mutant rescue, immunofluorescence |
Molecular biology of the cell |
High |
19109421
|
| 2009 |
Microtubule nucleation at the Golgi apparatus requires AKAP450, which binds the cis-side of the Golgi in a GM130-dependent manner. Depletion of GM130 disorganizes the AKAP450 network and impairs Golgi-based MT nucleation; brefeldin A redistributes AKAP450 to ER exit sites along with MT nucleation activity. |
siRNA knockdown, microtubule regrowth assay, immunofluorescence, brefeldin A treatment |
The EMBO journal |
High |
19242490
|
| 2010 |
PRMT5 localizes to the Golgi, forms complexes with GM130 and other Golgi ribbon/vesicle-tethering components, and methylates N-terminal arginines in GM130. PRMT5 depletion causes Golgi ribbon formation defects; arginine methylation of GM130 is critical for Golgi ribbon maintenance. |
Co-immunoprecipitation, in vitro methylation assay, siRNA knockdown, mutagenesis, immunofluorescence |
Cell research |
Medium |
20421892
|
| 2011 |
In mouse oocyte meiosis, GM130 localizes to spindle poles and midbody in a spindle-dependent manner; morpholino-mediated knockdown causes abnormal spindle formation, reduced polar body extrusion, impaired localization of γ-tubulin and Plk1 at MTOCs, aberrant spindle migration, and blocked p-MEK1/2 accumulation at spindle poles. |
Morpholino microinjection, immunofluorescence, live-cell imaging, nocodazole treatment |
Cell cycle (Georgetown, Tex.) |
Medium |
21552007
|
| 2013 |
WAC and GM130 directly interact at the Golgi; WAC binding to GM130 is required for autophagy. GM130 tethers GABARAP to the Golgi, inhibiting autophagy; WAC suppresses GM130 binding to GABARAP to allow centrosomal GABARAP delivery to the phagophore. Specifically, unlipidated and lipidated GABARAP (but not LC3B, GABARAPL1, or GATE-16) activates ULK kinase via the ULK1 LIR motif, revealing a non-hierarchical role for GABARAP in starvation-induced autophagy. |
Co-immunoprecipitation, siRNA knockdown, immunofluorescence, in vitro binding, ULK kinase assay |
Molecular cell |
High |
26687599
|
| 2014 |
GM130 forms a complex with RasGRF at the Golgi to regulate the Golgi pool of Cdc42. GM130 silencing causes RasGRF-dependent inhibition of Golgi Cdc42 (not plasma membrane Cdc42), disrupts asymmetric front-rear Cdc42-GTP distribution in migrating cells, and activates RasGRF-dependent Ras-ERK signaling. GM130 loss also induces E-cadherin downregulation indicative of EMT. |
Co-immunoprecipitation, Cdc42 activity (FRET) assay, siRNA knockdown, rescue experiments |
Nature communications |
Medium |
25208761
|
| 2014 |
In Drosophila dendrites, GM130 is responsible for connecting distinct Golgi compartments at soma and dendritic branch points; GM130 distribution determines the compartmental organization of dendritic Golgi outposts, which in turn regulates acentrosomal microtubule growth and dendritic branching. |
RNAi knockdown, immunofluorescence in vivo, live imaging, dendritic branching quantification |
Current biology : CB |
Medium |
24835455
|
| 2015 |
GM130 interacts with importin α via a classical nuclear localization signal (NLS) at mitotic entry, sequestering importin α on Golgi membranes. This releases the spindle assembly factor TPX2, which activates Aurora-A and stimulates local microtubule nucleation. GM130 also captures nascent microtubules, linking Golgi membranes to the spindle for organelle inheritance. |
Co-immunoprecipitation, immunofluorescence, mutagenesis of NLS, siRNA knockdown, microtubule regrowth assay |
Cell |
High |
26165940
|
| 2015 |
Crystal structure of GRASP65 PDZ domains in complex with the GM130 C-terminal peptide (1.96 Å resolution) reveals that GM130 simultaneously binds both PDZ1 and PDZ2 domains of GRASP65, contrary to prior models proposing only PDZ2 involvement. Mutagenesis experiments confirmed the structural observations. |
X-ray crystallography (1.96 Å), site-directed mutagenesis, co-immunoprecipitation |
The Journal of biological chemistry |
High |
26363069
|
| 2015 |
GM130 is a parallel homotetramer (not a homodimer as previously assumed) with a flexible rod-like structure exhibiting N-terminally open (Y-shaped) and closed (I-shaped) conformations, as revealed by biochemical and electron microscopic analyses. |
Gel filtration, electron microscopy, analytical ultracentrifugation |
The FEBS journal |
Medium |
25787021
|
| 2016 |
Targeted neuronal deletion of GM130 in mice causes Golgi fragmentation and defective positioning in Purkinje cells, impaired secretory trafficking, dendritic atrophy, reduced cerebellar size and Purkinje cell number, and progressive ataxia, demonstrating that Golgi dysfunction via GM130 loss is causally linked to neurodegeneration in vivo. |
Conditional knockout mice, immunofluorescence, electron microscopy, secretory trafficking assay, behavioral phenotyping |
Proceedings of the National Academy of Sciences of the United States of America |
High |
28028212
|
| 2017 |
GM130 knockout in mice causes globozoospermia; loss of GM130 does not affect secretion of pro-acrosomic vesicles but prevents their fusion into a single large acrosome vesicle. GM130 loss disrupts co-localization of adaptor protein complex AP1 and TGN46, suggesting GM130 is required for sorting and coating of Golgi-derived pro-acrosomic vesicles. |
Knockout mouse model, immunofluorescence, electron microscopy, co-localization analysis |
Cell death & disease |
Medium |
28055014
|
| 2019 |
Purified recombinant GM130 undergoes liquid-liquid phase separation into dynamic liquid-like droplets in near-physiological buffers at concentrations similar to its estimated local concentration at the cis-Golgi. Overexpressed GM130 also forms liquid droplets in cells. |
In vitro phase separation assay with recombinant protein, live-cell imaging of overexpressed protein |
FEBS letters |
Medium |
31833055
|
| 2021 |
CDK1-mediated phosphorylation of importin α at Ser-62 switches its substrate preference from TPX2 to GM130, thereby enabling GM130 to compete for importin α binding and locally activate TPX2 at the spindle pole area to promote astral microtubule growth and proper spindle orientation. |
Mutagenesis (importin α S62A), co-immunoprecipitation, astral microtubule growth assay, spindle orientation measurement |
Journal of cell science |
High |
33526712
|
| 2024 |
GM130 is a membrane-bound RNA-binding protein that directly recruits RNA and associated RNA-binding proteins to the Golgi membrane. RNA–GM130 condensates maintain the Golgi ribbon through liquid-liquid phase separation mediated by an intrinsically disordered N-terminal domain of GM130. Acute RNA degradation or GM130 loss disrupts the ribbon; GM130–RNA co-condensates are sufficient to link purified Golgi membranes in vitro. |
RNA-binding assay, acute RNA degradation (auxin-inducible degron for GM130), in vitro condensate reconstitution with purified membranes, deletion mutagenesis of IDR, live-cell imaging |
Nature cell biology |
High |
38992139
|
| 2002 |
GM130 interacts with the C-terminus of the HERG potassium channel in the Golgi; LQT2-causing HERG C-terminal mutations selectively disrupt this GM130 interaction. Overexpression of GM130 suppresses HERG current amplitude, suggesting GM130 functions as a checkpoint in HERG trafficking through the Golgi. |
Yeast two-hybrid, co-immunoprecipitation from HEK-293 cells, confocal co-localization, Xenopus oocyte current measurement |
The Journal of biological chemistry |
Medium |
12270925
|
| 2011 |
Bacterial effector EspG (from EPEC/EHEC) binds GM130 as identified by Y2H and confirmed by affinity co-purification and co-immunoprecipitation. EspG expression localizes to the Golgi and induces its fragmentation, disrupting protein secretion more potently than NleA/EspI. |
Yeast two-hybrid, affinity co-purification, co-immunoprecipitation, ectopic expression, secretion assay |
Cellular microbiology |
Medium |
21740499
|
| 2025 |
HIF-1α activation under hypoxia induces NEDD4-mediated ubiquitination and degradation of GM130, causing Golgi condensation. GM130 degradation promotes lipid accumulation and apolipoprotein A1 retention in intestinal epithelium. Inhibition of HIF-1α or NEDD4 prevents GM130 degradation and rescues Golgi structure and lipid trafficking. |
Hypoxia/HFD mouse model, co-immunoprecipitation, ubiquitination assay, HIF-1α inhibitor (PX-478), siRNA knockdown, apolipoprotein secretion assay |
Experimental & molecular medicine |
Medium |
39900792
|