| 2000 |
CLP-36 (PDLIM1) localizes to actin stress fibers in nonmuscle cells via its PDZ domain, which associates with the spectrin-like repeats of alpha-actinin. Both nonmuscle alpha-actinin-1 and alpha-actinin-4 form complexes with CLP-36, as demonstrated by immunoprecipitation and MALDI-TOF mass spectrometry. |
Co-immunoprecipitation, MALDI-TOF MS, subcellular localization by fluorescence microscopy, domain deletion analysis |
The Journal of biological chemistry |
High |
10753915
|
| 2000 |
Human CLP36 (PDLIM1) binds alpha-actinin-1 via its intervening sequence (not the PDZ or LIM domain alone), as shown by yeast two-hybrid analysis mapping to spectrin-like repeats 2 and 3 of alpha-actinin-1. CLP36 associates with actin filaments and stress fibers in activated platelets and endothelial cells and is absent from focal adhesions. The N-terminal PDZ domain plus intervening region, but not the LIM domain alone, targets CLP36 to stress fibers. |
Co-immunoprecipitation, pull-down assays, yeast two-hybrid, blot overlay, GFP fusion localization in endothelial cells |
Blood |
High |
11110697
|
| 2000 |
hCLIM1 (PDLIM1) interacts with alpha-actinin-2 (skeletal muscle isoform) via its LIM domain binding to the EF-hand region of alpha-actinin-2, defining a new mode of LIM domain interaction. hCLIM1 colocalizes with alpha-actinin at Z-disks in human myocardium. |
Yeast two-hybrid, co-immunoprecipitation, immunofluorescence colocalization |
Journal of cellular biochemistry |
Medium |
10861853
|
| 2002 |
CLP-36 (PDLIM1) acts as an adapter that recruits the novel kinase Clik1 to actin stress fibers via its C-terminal LIM domain. Clik1 is otherwise predominantly nuclear; association with CLP-36 relocalizes it to actin stress fibers, where it disrupts the periodic staining pattern of CLP-36. |
Yeast two-hybrid, subcellular colocalization, domain deletion analysis |
Journal of cell science |
Medium |
11973348
|
| 2007 |
CLP36 (PDLIM1) is required for actin stress fiber formation and focal adhesion assembly in BeWo cells. RNAi-mediated knockdown caused loss of stress fibers and focal adhesions; rescue required both the PDZ and LIM domains, establishing that both domains are functionally essential. |
RNAi knockdown, rescue with domain-deletion mutants, fluorescence microscopy |
Biochemical and biophysical research communications |
Medium |
17964547
|
| 2007 |
PDLIM1 (CLP36) is the PDZ domain-containing protein that tethers Plasma Membrane Ca2+-ATPase (PMCA) to the cytoskeleton in resting platelets via PDZ domain interactions with the C-terminal PDZ-binding motif of PMCA4b. CLP36, PMCA, alpha-actinin, and actin co-elute as a ~1,000 kDa complex by gel filtration, and CLP36 colocalizes with PMCA in both resting and activated platelets. |
Co-immunoprecipitation, LC-MS/MS, GST pull-down, gel filtration chromatography, immunofluorescence microscopy |
Thrombosis and haemostasis |
High |
17393022
|
| 2009 |
CLP36 (PDLIM1) interacts with palladin via its PDZ domain binding to the C-terminus of palladin. Palladin silencing suppresses CLP36 localization to stress fibers, and overexpression of the PDZ domain alone inhibits palladin localization to stress fibers. Alpha-actinin, CLP36, and palladin form a protein complex important for actin cytoskeleton regulation. |
Yeast two-hybrid, co-immunoprecipitation, siRNA knockdown, overexpression of domain constructs, fluorescence microscopy |
The FEBS journal |
Medium |
19366376
|
| 2009 |
CLP36 (PDLIM1) forms a complex with alpha-actinin in sensory (DRG) neurons, localizes to actin cytoskeleton in growth cones, and negatively regulates neurite outgrowth: RNAi knockdown of CLP36 induced lamellipodia and increased neurite length and number, whereas overexpression of the PDZ domain alone perturbed neurite outgrowth. |
RNAi, overexpression of deletion mutants, fluorescence microscopy, co-immunoprecipitation |
Journal of neurochemistry |
Medium |
19780892
|
| 2010 |
CLP36 (PDLIM1) interacts with palladin in dorsal root ganglion neurons, forming a complex detectable by co-immunoprecipitation; both proteins colocalize in neurites and cell bodies of primary DRG neurons. Sciatic nerve transection upregulates both CLP36 and palladin mRNAs, with CLP36 being more prominently upregulated, suggesting a specific role in nerve regeneration. |
Yeast two-hybrid, co-immunoprecipitation, immunofluorescence, qRT-PCR after nerve injury |
Neuroscience letters |
Medium |
20381583
|
| 2011 |
Alpha-actinin-4 and CLP36 (PDLIM1) form a complex in normal podocytes. siRNA depletion of alpha-actinin-4 markedly reduces CLP36 protein levels. FSGS-associated alpha-actinin-4 mutations (R310Q, Q348R) inhibit complex formation between alpha-actinin-4 and CLP36. Disruption of the alpha-actinin-4–CLP36 complex or reduction of CLP36 significantly inhibits RhoA activity and traction force generation in podocytes. |
Co-immunoprecipitation, siRNA knockdown, mutant overexpression, RhoA activity assay, traction force microscopy |
The Journal of biological chemistry |
High |
21680739
|
| 2011 |
PDLIM1 exists as part of a complex with FHL1, ACTN1, GSN (gelsolin), and ACTN4, identified by tandem affinity purification from HEK-293 cells and verified by co-immunoprecipitation from mouse heart ventricles and 3D fluorescence microscopy in adult cardiomyocytes. |
Tandem affinity purification, LC-MS, co-immunoprecipitation, 3D fluorescence microscopy |
Molecular bioSystems |
Medium |
21246116
|
| 2012 |
The LIM domain of PDLIM1 binds two zinc ions with femtomolar affinity (Kd avg ~2.5×10⁻¹⁴ M), and protein-protein interactions with the C-terminal extension further elevate Zn2+ affinity. Domain stability depends not only on zinc coordination but significantly on protein-protein interactions involving the C-terminus. |
Thermal denaturation, mass spectrometry, limited proteolysis, circular dichroism, zinc affinity measurements |
Journal of inorganic biochemistry |
High |
22922308
|
| 2012 |
CLP36 (PDLIM1) acts as a major inhibitor of GPVI/ITAM signaling in platelets. Mice expressing truncated CLP36 lacking the LIM domain or CLP36 knockout mice displayed hyperactivation (hyperphosphorylation, enhanced Ca2+ mobilization, granule secretion, integrin activation) specifically downstream of GPVI, leading to accelerated thrombus formation in vivo. |
Genetic knockout and truncation mouse models, platelet functional assays (Ca2+ mobilization, integrin activation, granule secretion), in vivo thrombosis models, phosphoprotein analysis |
Circulation research |
High |
22955732
|
| 2012 |
CLP36 and RIL (another ALP/Enigma family member) form a complex with alpha-actinin-1 and palladin on stress fibers. CLP36 depletion in F2408 fibroblasts caused non-oriented stress fiber organization; RIL compensated for this role. CLP36 and RIL have redundant roles in stress fiber formation but distinct effects on stress fiber dynamics. |
RNAi knockdown, time-lapse microscopy, co-immunoprecipitation, fluorescence microscopy |
Experimental cell research |
Medium |
22659164
|
| 2014 |
CLP36 (PDLIM1) promotes breast cancer cell migration and invasion through interaction with alpha-actinin-1 and alpha-actinin-4. Mutations abolishing alpha-actinin-binding activity eliminated the ability of CLP36 to promote migration. CLP36 depletion or disruption of the CLP36–alpha-actinin complex substantially inhibited Cdc42 activation, cell polarization, and directional migration. |
Co-immunoprecipitation, siRNA knockdown, binding-interface mutagenesis, Cdc42 GTPase activity assay, migration/invasion assays, in vivo metastasis model |
Oncogene |
High |
24662836
|
| 2015 |
PDLIM1 interacts with and stabilizes the E-cadherin/β-catenin complex at cell-cell junctions, thereby inhibiting β-catenin nuclear translocation and transcriptional activity and suppressing EMT in colorectal cancer cells. PDLIM1 knockdown increased nuclear β-catenin activity and promoted invasion, while overexpression attenuated EMT. |
Co-immunoprecipitation, siRNA knockdown, overexpression, β-catenin reporter assay, in vivo orthotopic and lung metastasis mouse models |
Cancer research |
High |
26701804
|
| 2015 |
PDLIM1 inhibits NF-κB-mediated inflammatory signaling by sequestering the p65 subunit of NF-κB in the cytoplasm in an IκBα-independent but alpha-actinin-4-dependent manner. PDLIM1 deficiency leads to increased nuclear p65 levels and enhanced proinflammatory cytokine production in response to innate stimuli. |
Co-immunoprecipitation, siRNA knockdown, subcellular fractionation, nuclear p65 quantification, cytokine ELISA |
Scientific reports |
Medium |
26679095
|
| 2015 |
PDLIM1 interacts with the neurotrophin receptor p75NTR (CD271) via its PDZ domain binding to the C-terminal SPV PDZ-binding motif of p75NTR. This interaction is regulated by S425 phosphorylation of p75NTR. The interaction also requires that p75NTR not be phosphorylated at S303 by PKA. shRNA knockdown of PDLIM1 completely ablated p75NTR-mediated glioma invasion in vitro and in vivo. |
Peptide-based interaction screen, co-immunoprecipitation, phosphorylation mutant analysis, shRNA knockdown, in vivo glioma invasion model |
Oncogene |
Medium |
26119933
|
| 2016 |
PDLIM1 must be degraded via the autophagy-lysosome pathway (dependent on ATG7) to allow proper cytoskeletal reorganization during spermatid differentiation. In atg7-null mice, PDLIM1 accumulates, impairing cytoskeleton organization and leading to defects in flagella biogenesis and cytoplasm removal during spermiogenesis. |
Conditional knockout mouse model (atg7-null), functional screening, western blot, phenotypic analysis of sperm morphology and motility |
Autophagy |
Medium |
27310465
|
| 2020 |
PDLIM1 competitively binds alpha-actinin-4 (ACTN4), leading to dissociation of ACTN4 from F-actin and preventing F-actin overgrowth. Loss of PDLIM1 induces excessive F-actin formation, resulting in dephosphorylation of LATS1 and activation of YAP, promoting HCC metastasis via the Hippo pathway. Asn145 (N145) of PDLIM1 is critical for its interaction with ACTN4, and N145A mutation abolishes this regulatory function. |
Co-immunoprecipitation, site-directed mutagenesis (N145A), F-actin binding assay, LATS1 phosphorylation assay, YAP activity measurement, in vitro invasion and in vivo metastasis models |
Hepatology (Baltimore, Md.) |
High |
31509262
|
| 2020 |
PDLIM1 localizes to actin-rich structures generated by bacterial pathogens: it accumulates at sites of Listeria entry, in actin clouds surrounding immotile bacteria, and within actin comet/rocket tails. PDLIM1 is maintained in the actin core of membrane protrusions but absent from the membrane invagination internalizing Listeria. PDLIM1 is also a component of EPEC pedestals and its recruitment is dependent on the bacterial effector Tir. |
Immunofluorescence microscopy, subcellular localization during bacterial infection, Tir-deletion bacterial mutant analysis |
Anatomical record (Hoboken, N.J. : 2007) |
Medium |
33022122
|
| 2022 |
CLP36 (PDLIM1) promotes p53-deficient sarcoma progression by inhibiting AIP-4 (ITCH E3 ligase)-dependent proteasomal degradation of YAP1, thereby increasing YAP1 protein levels. CLP36 knockout in mice markedly inhibited p53-deficiency-induced tumorigenesis. |
Co-immunoprecipitation, genetic KO mouse model, ubiquitination assay, western blot, tumor growth assay |
Theranostics |
Medium |
35836803
|
| 2023 |
PDLIM1 interacts with hexokinase 2 (HK2) in gastric cancer cells, as demonstrated by co-immunoprecipitation. This interaction mediates glycolysis and cell biological behaviors under glucose deprivation through the Wnt/β-catenin signaling pathway. |
Co-immunoprecipitation, glucose metabolism assays (glycolytic indicators), western blot, siRNA knockdown and overexpression |
Cell and tissue research |
Low |
37930472
|
| 2025 |
Cblb (an E3 ubiquitin ligase) binds to the PDZ and LIM domains of PDLIM1 and ubiquitinates PDLIM1 at K244, targeting it for proteasome-mediated degradation. In microglia, this Cblb-mediated degradation of PDLIM1 releases NF-κB signaling, promoting pyroptosis. Botulinum toxin A suppresses Cblb activity, thereby preventing PDLIM1 degradation and inhibiting NF-κB-mediated pyroptosis. |
Mass spectrometry, co-immunoprecipitation, ubiquitination assay (K244 site identification), proteasome inhibition, shRNA knockdown, lentiviral/AAV rescue experiments in vivo |
The journal of headache and pain |
Medium |
40696327
|