| 2002 |
GOPC is predominantly localized at the trans-Golgi region in round spermatids; GOPC-deficient male mice are infertile with globozoospermia due to fragmentation of acrosomes in early round spermatids — abnormal vesicles fail to fuse to developing acrosomes — establishing GOPC as essential for acrosomal vesicle fusion during spermiogenesis. |
Gene knockout mouse (GOPC-deficient), electron microscopy, immunofluorescence, intracytoplasmic sperm injection (ICSI) |
Proceedings of the National Academy of Sciences of the United States of America |
High |
12149515
|
| 2001 |
GOPC (PIST) directly and specifically binds TC10:GTP (a Rho-family GTPase) via a leucine zipper-containing coiled-coil domain; the first coiled-coil and PDZ domains are not required for TC10 binding, but deletion of the N-terminal portion of the leucine zipper abolishes dimerization. GOPC also forms homodimers. |
Yeast two-hybrid, in vitro binding assays, deletion mutagenesis |
Biochemical and biophysical research communications |
Medium |
11162552
|
| 2001 |
GOPC interacts with frizzled via the PDZ domain of GOPC and the C-terminal Ser/Thr-X-Val motif of frizzled, both in vivo and in vitro; GOPC and frizzled colocalize at the Golgi apparatus, and coexpression of GOPC with frizzled causes translocation of GOPC to the plasma membrane. Brefeldin A disrupts both GOPC Golgi localization and frizzled plasma membrane targeting, indicating GOPC participates in vesicle transport of frizzled from Golgi to plasma membrane. |
Co-immunoprecipitation, in vitro binding, immunofluorescence, deletion mutagenesis, brefeldin A treatment |
Biochemical and biophysical research communications |
Medium |
11520064
|
| 2005 |
GOPC (PIST) interacts with somatostatin receptor subtype 5 (SSTR5) via the PDZ ligand motif at the receptor's C-terminus and retains SSTR5 in the Golgi apparatus when coexpressed. Endogenous SSTR5 in AtT-20 cells colocalizes with PIST in the Golgi. Removal of the PDZ ligand motif inhibits receptor recycling to the plasma membrane after agonist washout, indicating PIST/GOPC is required for postendocytic sorting of SSTR5. |
Yeast two-hybrid, coexpression/immunofluorescence, deletion mutagenesis, cell-surface recycling assay |
The Journal of biological chemistry |
Medium |
16012170
|
| 2005 |
GOPC (PIST) interacts with golgin-160 via an internal coiled-coil region of PIST and a leucine-rich repeat within golgin-160; they colocalize to Golgi membranes and interact in vivo. A widely expressed isoform, golgin-160B, lacks the leucine repeat and cannot bind PIST. |
Yeast two-hybrid, GST pulldown, co-immunoprecipitation, immunofluorescence colocalization, isoform cloning |
The Journal of biological chemistry |
High |
15951434
|
| 2006 |
GOPC (PIST) PDZ domain solution structure was solved by NMR; it is a canonical class I PDZ domain with two alpha-helices and six beta-strands. Chemical shift perturbation experiments showed the GOPC PDZ domain binds the C-terminal motif of neuroligin in fast exchange with low affinity, and a 3D complex model was constructed by molecular dynamics simulation. |
NMR structure determination, chemical shift perturbation, molecular dynamics simulation |
Protein science : a publication of the Protein Society |
High |
16882988
|
| 2006 |
GOPC (PIST) binds Rhotekin via its PDZ domain interacting with the C-terminal SPV motif of Rhotekin; this interaction occurs in vitro and in MDCK cells. Activated Rho markedly inhibits the Rhotekin-PIST interaction. PIST and Rhotekin colocalize at the Golgi in non-polarized cells and at adherens junctions in polarized cells, and PIST is involved in recruiting Rhotekin to adherens junctions. |
Yeast two-hybrid, in vitro binding, co-immunoprecipitation, immunofluorescence, dominant-active Rho expression |
The Biochemical journal |
Medium |
16646955
|
| 2010 |
GOPC (PIST) binds cadherin 23 (CDH23) via the PIST PDZ domain and the C-terminal PDZ domain-binding interface of CDH23, retaining CDH23 in the trans-Golgi network. Co-expression of MAGI-1 or harmonin releases CDH23 from PIST retention, suggesting competitive displacement. |
Co-immunoprecipitation, immunofluorescence colocalization, TGN retention assay, competitive coexpression |
BMC cell biology |
Medium |
20958966
|
| 2011 |
GOPC PDZ domain binds the C-terminal PDZ motif of transmembrane mucin MUC3. GOPC overexpression downregulates total MUC3 levels, and this effect is reversed by co-introduction of CFTR, indicating CFTR and MUC3 compete for GOPC binding. GOPC also directs CFTR for degradation. |
PDZ domain binding screen (123 PDZ domains), co-immunoprecipitation, overexpression with protein level assays |
Journal of cell science |
Medium |
21852426
|
| 2013 |
GOPC (PIST) mediates a PDZ domain-dependent interaction with the voltage-gated potassium channel KV10.1, enhancing KV10.1 surface levels. The functional (but not physical) interaction requires both coiled-coil and PDZ domains of PIST. The neural isoform nPIST interacts physically but does not alter KV10.1 surface expression. A short isoform sPIST lacks PDZ domain, does not co-precipitate with KV10.1, but reduces KV10.1 surface expression in a dominant-negative manner. |
Co-immunoprecipitation from native and expression systems, surface expression assay, isoform cloning and expression, domain mutagenesis |
Frontiers in physiology |
Medium |
23966943
|
| 2013 |
GOPC (PIST) interacts with NaPi-2a (sodium-phosphate transporter) in the trans-Golgi network during retrograde trafficking from the plasma membrane. PIST overexpression retains NaPi-2a in the TGN and inhibits Na-dependent phosphate transport in OK cells, and prevents adaptation to low-phosphate medium. |
Co-immunoprecipitation, immunofluorescence, phosphate transport functional assay, overexpression in OK cells |
BioMed research international |
Medium |
23509734
|
| 2015 |
GOPC (PIST) controls β1-adrenergic receptor (β1AR) trafficking in both anterograde (biosynthetic) and postendocytic pathways. PIST overexpression retains β1AR in the trans-Golgi network and reduces MAPK signaling by agonist; coexpression with PSD-95 releases receptors to the plasma membrane. cAMP pathway activation relocalizes PIST from TGN to SNX1-positive endosomes where it colocalizes with internalized β1AR and protects receptors from lysosomal degradation. β1AR levels are decreased in hippocampi of PIST-deficient mice. |
Overexpression/knockdown, immunofluorescence colocalization, MAPK signaling assay, PIST-KO mouse brain analysis |
The Journal of biological chemistry |
High |
25614626
|
| 2015 |
GOPC localizes to the trans-Golgi network (TGN) in MDCK cells, colocalizing with Rab5 and Rab14 but not Rab11. Knockdown of GOPC decreases transepithelial resistance, increases paracellular flux, and reduces lateral claudin-1 labeling and claudin-2 protein levels, indicating GOPC is required for trafficking of tight junction components from the TGN. |
Immunofluorescence colocalization, siRNA knockdown, transepithelial resistance measurement, paracellular flux assay, western blot |
Cell and tissue research |
Medium |
25616555
|
| 2016 |
GOPC (PIST) interacts with protocadherin 15 (PCDH15) via the PDZ domain of PIST and the C-terminal PDZ domain-binding interface of PCDH15, retaining PCDH15 in the trans-Golgi network and reducing its membrane expression. |
Co-immunoprecipitation, immunofluorescence, TGN retention assay |
Neural plasticity |
Low |
27867666
|
| 2020 |
HSV-1 protein pUL56 directly binds GOPC, stimulates its ubiquitination and proteasomal degradation. pUL56-mediated GOPC degradation alters cell-surface proteome of infected cells, including loss of TLR2 surface expression, which is GOPC-dependent. |
Quantitative multiplexed proteomics (TMT), plasma membrane profiling, co-immunoprecipitation, ubiquitination assay, proteasome inhibitor experiments |
Cell reports |
High |
33027661
|
| 2020 |
GOPC interacts with the GTPase ARFRP1 at the trans-Golgi network and together they regulate plasma membrane localization of the SNARE protein SNAP25; knockdown of both GOPC and ARFRP1 in Min6 cells reduces SNAP25 plasma membrane localization and enhances its degradation, impairing glucose-stimulated insulin secretion. Overexpression of SNAP25 or GOPC restores insulin secretion in β-cell-specific Arfrp1-KO islets. |
Pulldown with mass spectrometry, co-immunoprecipitation, super-resolution microscopy, siRNA knockdown, glucose-stimulated insulin secretion assay, KO mouse |
Molecular metabolism |
High |
33359402
|
| 2021 |
GOPC (Gopc) is required for synaptic targeting of mGluR5 and neuroligin 1 (Nlgn1) in neurons; knockdown in primary cultured neurons and conditional KO mouse both show impaired plasma membrane targeting of mGlu5 and Nlgn1, while NMDA receptors were unaffected. In Gopc KO hippocampus/cortex, mGlu5 targeting to postsynaptic density is reduced, coinciding with alterations in mGluR-dependent synaptic plasticity and deficits in contextual fear conditioning. |
shRNA knockdown in primary neurons, conditional KO mouse, immunofluorescence, synaptic fractionation, mGluR-dependent LTD assay, contextual fear conditioning |
Molecular neurobiology |
High |
34383253
|
| 2022 |
GOPC is required for correct basolateral targeting of syndecan-1 in polarized MDCK cells via interaction with syndecan-1's full-length PDZ motif; this sorting is not dependent on transmembrane domain or sphingomyelin content. GOPC overexpression also alters Golgi morphology, suggesting GOPC affects sorting indirectly through effects on Golgi organization. |
siRNA knockdown, domain mutagenesis, trafficking/sorting assay in polarized MDCK cells, Golgi morphology imaging |
Molecular biology of the cell |
Medium |
35830596
|
| 2024 |
GOPC (PIST) traffics from the Golgi to parasitophorous vacuoles (PVs) during Leishmania major infection and associates with autophagy regulatory protein Beclin 1 within PVs (but not with LC3). siRNA silencing of PIST increases parasite burden; PIST overexpression restricts L. major infectivity, establishing PIST as a regulator of Leishmania infection via the Beclin 1-PI3KC3 autophagy pathway. |
Immunofluorescence colocalization, co-immunoprecipitation, siRNA knockdown, overexpression, parasite burden quantification |
ACS infectious diseases |
Medium |
38556987
|
| 2025 |
MC-LR toxin induces proteasomal degradation of GOPC by promoting excessive ubiquitination via dual inhibition of the deubiquitinase UCHL3: MC-LR directly binds the catalytic domain of UCHL3, blocking its interaction with GOPC and inhibiting its enzymatic activity, while also suppressing UCHL3 transcription and destabilizing UCHL3 protein. UCHL3 dysfunction leads to GOPC ubiquitination and destruction, disrupting acrosome biogenesis. |
In vitro binding assay (MC-LR to UCHL3 catalytic domain), ubiquitination assays, co-immunoprecipitation, transcription analysis, protein stability assays |
Environmental pollution |
Medium |
40784473
|
| 2025 |
Leishmania GP63 metalloprotease facilitates PIST-Golgin160 complex formation by suppressing caspase-3 activation, thereby preventing Golgin160 cleavage. GP63 recruits PIST to parasitophorous vacuoles and promotes PIST-Beclin1 colocalization while excluding LC3. |
Co-immunoprecipitation, immunofluorescence, GP63-deficient parasite comparison, caspase inhibitor (Z-VAD-FMK) treatment |
ACS infectious diseases |
Medium |
41269215
|
| 2025 |
GOPC-ROS1 fusion enhances the catalytic activity of the ROS1 receptor tyrosine kinase fragment and alters the tyrosine phosphorylation profile in human lymphatic endothelial cells. Impaired phosphorylation of ZO-1 at tyrosine 895, due to decreased colocalization of GOPC-ROS1 with ZO-1, inhibits tight junction formation in lymphatic endothelial cells. |
Phosphoproteomic profiling, overexpression of fusion protein, colocalization assay, ZO-1 phosphorylation site mutagenesis/validation |
Biochemical pharmacology |
Medium |
40819798
|
| 2025 |
Using affinity purification mass spectrometry, SHP2 was identified in direct interaction with GOPC-ROS1 (and other ROS1 fusion oncoproteins) but not with ALK fusion oncoproteins; ROS1 fusions phosphorylate SHP2 to a greater extent than ALK fusions, suggesting non-canonical SHP2-driven signaling downstream of GOPC-ROS1. |
Affinity purification mass spectrometry, phosphoproteomics |
bioRxivpreprint |
Low |
bio_10.1101_2025.05.27.656302
|
| 2013 |
The coiled-coil domain of PIST (amino acids 29-133) was crystallized and X-ray diffraction data collected to 4.0 Å resolution (hexagonal space group P6₂22 or P6₄22); this domain is responsible for interaction with Rab6A and fusion with ROS1. |
Protein crystallization, X-ray diffraction |
Acta crystallographica Section F |
Low |
23545662
|