Affinage

KIRREL1

Kin of IRRE-like protein 1 · UniProt Q96J84

Length
757 aa
Mass
83.5 kDa
Annotated
2026-04-28
34 papers in source corpus 24 papers cited in narrative 24 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

KIRREL1 (NEPH1) is a transmembrane immunoglobulin superfamily protein that functions as a core structural and signaling component of the glomerular slit diaphragm and as a cell-surface activator of the Hippo tumor-suppressor pathway. At the podocyte slit diaphragm, KIRREL1 forms glycosylation-dependent heterodimers with nephrin via extracellular Ig domains and binds ZO-1 through a C-terminal PDZ-binding motif, assembling an adhesion–scaffolding complex essential for filtration barrier integrity; genetic deletion causes foot process effacement and proteinuria, and homozygous loss-of-function mutations in humans cause steroid-resistant nephrotic syndrome (PMID:11416156, PMID:12865409, PMID:12660326, PMID:31472902). Fyn kinase phosphorylates KIRREL1 on cytoplasmic tyrosines (including Y637/Y638), creating docking sites for Grb2 and Csk, regulating the KIRREL1–ZO-1 interaction as a phosphorylation-dependent switch, and cooperating with nephrin–Nck signaling to drive actin polymerization at intercellular junctions, while the motor protein Myo1c mediates KIRREL1 vesicular trafficking to the plasma membrane (PMID:17923684, PMID:18258597, PMID:18922801, PMID:21402783). Independent of its renal role, KIRREL1 directly binds SAV1 and LATS1/2 at cell–cell contacts to promote Hippo pathway kinase activation and YAP/TAZ suppression, forming a TEAD-dependent negative feedback loop; its loss enhances YAP-driven hepatocyte reprogramming and tumor growth in vivo (PMID:35177623, PMID:36044856, PMID:35704761).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 2001 High

    Establishing that KIRREL1 is essential for podocyte foot process integrity resolved the gene's primary physiological role: its deletion causes slit diaphragm loss and proteinuria, proving it is not redundant with nephrin.

    Evidence Gene-trap knockout mouse with electron microscopy phenotyping

    PMID:11416156

    Open questions at the time
    • Molecular partners at the slit diaphragm were unknown
    • Whether KIRREL1 functions as an adhesion molecule or solely as a signaling receptor was unclear
  2. 2002 High

    Identification of the KIRREL1–podocin interaction and its dependence on a central tyrosine residue established the first cytoplasmic signaling link, suggesting KIRREL1 operates within a multi-protein slit diaphragm signaling complex.

    Evidence Reciprocal co-immunoprecipitation with site-directed mutagenesis and AP-1 reporter assays

    PMID:12424224

    Open questions at the time
    • Downstream signaling pathways were not defined
    • Whether podocin interaction is required in vivo was untested
  3. 2003 High

    Demonstrating that KIRREL1 forms direct heterodimers with nephrin (via extracellular Ig domains) and binds ZO-1 (via PDZ interaction), and that disrupting these complexes in vivo causes proteinuria, defined the core molecular architecture of the slit diaphragm as a KIRREL1–nephrin–ZO-1 ternary complex.

    Evidence Immunogold EM localization, reciprocal co-IP of native and recombinant proteins, in vivo antibody injection, truncation/glycosylation analysis

    PMID:12646566 PMID:12660326 PMID:12865409

    Open questions at the time
    • Stoichiometry and geometry of the nephrin–KIRREL1 heterodimer were unresolved
    • Whether glycosylation-dependent binding reflects a quality-control or a regulatory mechanism was unknown
  4. 2007 High

    Identifying Fyn-mediated tyrosine phosphorylation of KIRREL1 and its recruitment of Grb2 to cooperate with nephrin–Nck in actin polymerization answered how KIRREL1 transduces extracellular adhesion into cytoskeletal remodeling at podocyte junctions.

    Evidence In vitro kinase assay, phosphosite mutagenesis, actin polymerization assays at the plasma membrane

    PMID:17923684

    Open questions at the time
    • In vivo relevance of individual phosphosites had not been tested genetically
    • Upstream signals triggering Fyn activation at the slit diaphragm were unknown
  5. 2008 High

    Mapping specific phosphorylation sites (Y637/Y638) and showing that ischemia disrupts the KIRREL1–ZO-1 interaction while Fyn-dependent re-phosphorylation restores it established tyrosine phosphorylation as a molecular switch controlling slit diaphragm assembly and repair.

    Evidence Peptide mass fingerprinting, site-directed mutagenesis, rat ischemia model and ATP-depletion injury model with co-IP

    PMID:18258597 PMID:18922801

    Open questions at the time
    • Which phosphatase reverses the switch was not identified at this time
    • Whether phosphorylation-dependent ZO-1 binding is required for barrier function in vivo remained untested
  6. 2009 High

    Discovery that KIRREL1 suppresses surface expression of BK (Slo1) channels in podocytes and neurons revealed an unexpected function as a regulator of ion channel trafficking, extending its role beyond structural adhesion.

    Evidence Reciprocal co-IP from endogenous podocyte and neuronal lysates, siRNA knockdown, whole-cell electrophysiology

    PMID:19794150

    Open questions at the time
    • Mechanism by which KIRREL1 retains Slo1 intracellularly was not determined
    • Physiological consequence for kidney filtration or neuronal excitability in vivo was not tested
  7. 2011 High

    Showing that Myo1c directly binds KIRREL1 and transports it to the cell membrane answered how KIRREL1 reaches the slit diaphragm, and that KIRREL1 independently promotes cell adhesion in trans (while nephrin requires KIRREL1 for adhesion) clarified the hierarchy of slit diaphragm assembly.

    Evidence Co-IP, dominant-negative/siRNA Myo1c with FRAP and TER assays; L-fibroblast trans-adhesion assay

    PMID:21306299 PMID:21402783

    Open questions at the time
    • Whether Myo1c delivers KIRREL1 via a specific vesicular compartment was uncharacterized
    • Structural basis of the Myo1c–KIRREL1 interface was not yet resolved
  8. 2012 High

    Determining the solution structure of the KIRREL1 cytoplasmic domain and identifying critical ZO-1-binding residues (K761, Y762) by SWAXS and mutagenesis provided the first atomic-resolution view of the KIRREL1–ZO-1 interface.

    Evidence SWAXS structural determination, alanine-scanning mutagenesis with in vivo/in vitro pulldown validation

    PMID:22262837

    Open questions at the time
    • Full-length extracellular domain structure remained unresolved
    • How phosphorylation at nearby sites alters the structural conformation was not addressed
  9. 2016 High

    SAXS-based structural modeling of the Myo1c–KIRREL1 complex and identification of a single point mutation that abolishes binding defined the molecular interface for KIRREL1 membrane trafficking.

    Evidence SAXS structural modeling, site-directed mutagenesis, FRAP live-cell imaging

    PMID:27044863

    Open questions at the time
    • Whether other motors compensate in the Myo1c-binding mutant in vivo was unknown
    • Regulation of Myo1c–KIRREL1 binding (e.g., by calcium or phosphorylation) was not explored
  10. 2019 Medium

    Identification of homozygous KIRREL1 mutations causing steroid-resistant nephrotic syndrome in humans, with mutant proteins failing to reach the cell surface, translated the mouse knockout phenotype to a defined human Mendelian disease and confirmed trafficking as a disease-relevant mechanism.

    Evidence Human genetic analysis with functional membrane localization assay in podocytes

    PMID:31472902

    Open questions at the time
    • Number of independent families was limited
    • Whether these mutations also affect Hippo pathway signaling in patients was not explored
  11. 2021 High

    Demonstrating that HGF binds KIRREL1 extracellularly with high affinity and induces its phosphorylation independently of MET identified KIRREL1 as a novel HGF receptor that mediates podocyte repair, with SHP-2 serving as the counteracting phosphatase.

    Evidence Surface plasmon resonance with purified proteins, phosphorylation assays, cultured podocytes and ex vivo Drosophila nephrocytes

    PMID:34391780

    Open questions at the time
    • Whether HGF–KIRREL1 signaling is relevant to Hippo pathway regulation was not tested
    • In vivo mammalian validation of HGF-dependent podocyte repair via KIRREL1 was lacking
  12. 2022 High

    Three independent studies converged to show that KIRREL1 directly binds SAV1 and LATS1/2, activating the Hippo kinase cascade to suppress YAP/TAZ, and that YAP/TAZ transcriptionally induces KIRREL1, forming a negative feedback loop — establishing KIRREL1 as a cell-surface tumor suppressor upstream of Hippo signaling.

    Evidence Reciprocal co-IP, CRISPR knockout, YAP reporter assays, in vivo CRISPR screen, LATS kinase activity assays, mouse liver regeneration and cholangiocarcinoma models

    PMID:35177623 PMID:35704761 PMID:36044856

    Open questions at the time
    • How KIRREL1 simultaneously engages nephrin at the slit diaphragm and SAV1/LATS in Hippo signaling — whether these are tissue-context-dependent or co-occurring — is unresolved
    • Structural basis of the KIRREL1–SAV1 interaction is unknown
    • Whether KIRREL1's Hippo function requires its extracellular adhesion or only its cytoplasmic domain was not dissected
  13. 2024 Medium

    Demonstrating that KIRREL1 is required for neurite branching in dorsal horn neurons and is transcriptionally regulated by PRRXL1 via intronic binding extended its function beyond kidney and liver to nervous system development.

    Evidence ChIP for PRRXL1 binding to Neph1 intronic regions, loss-of-function neurite morphometry

    PMID:39049046

    Open questions at the time
    • Whether the same Fyn/Grb2 signaling axis operates in neurons is untested
    • In vivo behavioral or circuit-level consequences of neuronal KIRREL1 loss are not characterized

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include the high-resolution structure of the full extracellular nephrin–KIRREL1 heterodimer, how KIRREL1 partitions between its slit diaphragm, Hippo, and neuronal functions in different tissues, and whether its HGF receptor and Hippo activator roles intersect.
  • No high-resolution crystal or cryo-EM structure of full-length KIRREL1 or the nephrin–KIRREL1 complex exists in the peer-reviewed literature
  • Mechanism by which tissue context determines KIRREL1's partner selection (nephrin vs. SAV1/LATS) is unknown
  • Whether the HGF–KIRREL1 axis modulates YAP activity in injured podocytes has not been tested

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0098631 cell adhesion mediator activity 4 GO:0060089 molecular transducer activity 3 GO:0098772 molecular function regulator activity 3
Localization
GO:0005886 plasma membrane 5 GO:0031410 cytoplasmic vesicle 2
Pathway
R-HSA-162582 Signal Transduction 7 R-HSA-1500931 Cell-Cell communication 4 GO:0001618 virus receptor activity 1 R-HSA-1266738 Developmental Biology 1
Partners
FYNGRB2LATS1MYO1CNPHS1NPHS2SAV1TJP1
Complex memberships
Hippo pathway SAV1-LATS complexslit diaphragm complex (nephrin-NEPH1-ZO-1)

Evidence

Reading pass · 24 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2001 NEPH1 (KIRREL1) is expressed in glomerular podocytes and its genetic deletion in mice causes effacement of podocyte foot processes and severe proteinuria, establishing an essential role in maintaining the glomerular filtration barrier. Gene trap knockout mouse, electron microscopy, Northern analysis Molecular and cellular biology High 11416156
2002 NEPH1 interacts with the C-terminal domain of podocin via a conserved binding motif; mutation of a centrally located tyrosine residue in NEPH1 dramatically reduces its affinity for podocin. NEPH1 also triggers AP-1 activation requiring Tec family kinases. Co-immunoprecipitation, site-directed mutagenesis, reporter assays FASEB journal High 12424224
2003 Neph1 localizes to the glomerular slit diaphragm by immunogold electron microscopy and directly interacts with nephrin (via extracellular segments) and ZO-1 (via ZO-1 PDZ domains with Neph1 cytoplasmic tail). Disrupting the Neph1-nephrin interaction in vivo causes proteinuria and loss of ZO-1 protein expression. Immunogold electron microscopy, native and recombinant protein co-immunoprecipitation, in vivo antibody injection model The Journal of clinical investigation High 12865409
2003 Neph1 localizes exclusively to lateral margins of podocyte foot processes at the slit diaphragm insertion. Neph1 and Nephrin form direct cis-heterodimeric interactions involving both their cytoplasmic domains and their extracellular domains; Neph1 does not homodimerize via its extracellular domain. Immunogold electron microscopy, detergent-resistant membrane fractionation, co-immunoprecipitation The Journal of biological chemistry High 12646566
2003 NEPH1 forms homodimers and heterodimers with nephrin through promiscuous Ig-domain interactions; two Ig domains of either protein are sufficient for binding. These interactions are strictly dependent on post-translational glycosylation. Co-immunoprecipitation, NEPH1-IgG fusion protein pulldown, truncation analysis, overexpression in HEK293T cells Journal of the American Society of Nephrology High 12660326
2006 Neph1 is expressed at synaptic sites in the mouse brain (including hippocampus CA1/CA3) and interacts with the PDZ domain of the synaptic scaffold CASK via its cytoplasmic tail, suggesting a role in synaptogenesis. In situ hybridization, immunohistochemistry, immunogold electron microscopy, co-immunoprecipitation/PDZ domain pulldown The Journal of comparative neurology Medium 16874800
2007 Neph1 is phosphorylated on specific tyrosine residues by the Src family kinase Fyn, leading to recruitment of the adaptor Grb2. Neph1-Nephrin direct interaction juxtaposes Grb2 and Nck1/2 at the membrane to cooperatively promote actin polymerization at the podocyte intercellular junction. In vitro kinase assay, site-directed mutagenesis of phosphorylation sites, co-immunoprecipitation, actin polymerization assays at plasma membrane Molecular and cellular biology High 17923684
2008 Neph1 is phosphorylated in vivo by Src family kinase Fyn on multiple tyrosine residues including Y637 and Y638; phosphorylation-dependent binding of Neph1 to adaptor Grb2 and kinase Csk was demonstrated from rat glomerular lysates. Neph1 attenuates Fyn-elicited ERK activation through its Grb2-binding motif. In vitro kinase assay, peptide mass fingerprinting, site-directed mutagenesis, pulldown from glomerular lysates, ERK signaling assays The Journal of biological chemistry High 18258597
2008 Renal ischemia causes rapid dissociation of the Neph1-ZO-1 interaction; recovery restores interaction dependent on Fyn-mediated tyrosine phosphorylation of Neph1. Tyrosine phosphorylation of Neph1 significantly increases Neph1-ZO-1 binding, establishing phosphorylation as a switch controlling this complex. In vivo rat ischemia model, cell culture ATP-depletion injury model, co-immunoprecipitation, immunofluorescence The Journal of biological chemistry High 18922801
2009 Neph1 interacts with large-conductance Ca2+-activated K+ channels (Slo1/BK) encoded by Slo1, demonstrated by reciprocal co-immunoprecipitation from endogenous podocyte and ciliary ganglion neuron proteins. Neph1 suppresses steady-state surface expression of Slo1 in podocytes and neurons, while siRNA knockdown of Neph1 in neurons increases Slo1 surface expression and BKCa current. Reciprocal co-immunoprecipitation from endogenous cells, GST pulldown, cell surface biotinylation, siRNA knockdown, whole-cell electrophysiology American journal of physiology. Cell physiology High 19794150
2011 Motor protein Myo1c directly interacts with Neph1 in an actin-dependent manner and facilitates transport of Neph1 to the podocyte cell membrane; dominant-negative Myo1c or Myo1c knockdown significantly reduces Neph1 membrane localization and impairs tight junction formation and cell migration. In vivo and in vitro co-immunoprecipitation, dominant-negative overexpression, siRNA knockdown, live-cell imaging, transepithelial electric resistance assay Molecular and cellular biology High 21402783
2011 Neph1 and Neph3 independently induce cell adhesion, while nephrin requires trans-interaction with Neph1 or Neph3 to promote cell-cell contact formation. Trans-interaction of nephrin with Neph1 or Neph3 down-regulates tyrosine phosphorylation of nephrin. L-fibroblast cell adhesion assay, co-immunoprecipitation for heterodimerization, phosphorylation analysis The Biochemical journal Medium 21306299
2012 Solution structure of the Neph1 cytoplasmic domain (Neph1-CD) determined by SWAXS; structural modeling of the Neph1-CD·ZO-1-PDZ1 complex identified that residues Lys-761 and Tyr-762 in Neph1 (in addition to C-terminal Thr-His-Val) are critical for ZO-1 binding, validated by alanine-scanning mutagenesis. Small/wide angle X-ray scattering (SWAXS), circular dichroism, in vivo and in vitro pulldown, site-directed mutagenesis The Journal of biological chemistry High 22262837
2014 Inhibiting Neph1 signaling by transducing its cytoplasmic domain (Neph1-CD) into podocytes prevents puromycin aminonucleoside (PAN)-induced phosphorylation of Neph1, retains Neph1 in lipid raft fractions and at the membrane, and protects podocytes from cytoskeletal damage and albumin leakage. Protein transduction domain approach, subcellular fractionation, immunofluorescence, in vivo zebrafish injury model The Journal of biological chemistry Medium 24554715
2016 Myo1c binds Neph1 at its C-terminal tail domain, as demonstrated by SAXS structural modeling showing an extended S-shaped Myo1c with Neph1 attached. A single point mutation in Neph1 at the identified interaction surface abolishes Myo1c binding in vitro and in live-cell assays. FRAP demonstrates Myo1c-dependent intracellular vesicular movement and membrane turnover of Neph1. Small angle X-ray scattering, site-directed mutagenesis, in vitro and live-cell binding assays, FRAP live-cell imaging Molecular and cellular biology High 27044863
2017 CD80 interacts with Neph1 via their extracellular domains, demonstrated by pulldown assays in HEK293 cells; CD80 co-localizes with Neph1 in podocytes and its overexpression causes actin derangement. Co-immunoprecipitation/pulldown in HEK293 cells, immunofluorescence co-localization Clinical and experimental nephrology Low 29022109
2017 Stabilizing the Neph1-ZO-1 protein-protein interaction using the small molecule isodesmosine (ISD) enhances Neph1-ZO-1 binding in vitro and in vivo, and protects podocytes from injury-induced loss of transepithelial permeability in cell culture, mouse, and zebrafish models. Structural pocket screening, small molecule binding assays, biochemical binding analysis, TER assays, in vivo mouse and zebrafish models Scientific reports Medium 28935902
2019 Homozygous mutations in KIRREL1 cause steroid-resistant nephrotic syndrome; mutant KIRREL1 proteins fail to localize to the podocyte cell membrane, indicating defective trafficking and impaired podocyte function. Human genetic analysis, functional assessment of mutant protein membrane localization in podocytes Kidney international Medium 31472902
2021 NEPHRIN and NEPH1 are novel receptor proteins for hepatocyte growth factor (HGF); HGF binds their extracellular domains with high affinity (surface plasmon resonance), induces their phosphorylation independently of the MET receptor, and SHP-2 (PTPN11) mediates their dephosphorylation. HGF-induced phosphorylation of NEPHRIN and NEPH1 promotes podocyte repair. Surface plasmon resonance, baculovirus-expressed recombinant proteins, phosphorylation assays, molecular modeling, in vitro cultured podocytes, ex vivo Drosophila nephrocytes, chemical injury models The Journal of biological chemistry High 34391780
2022 KIRREL1 physically interacts with SAV1 and recruits SAV1 to cell-cell contact sites, acting as a positive upstream regulator of the Hippo pathway. Knockout of KIRREL1 increases YAP activity in neighboring cells. During liver regeneration, KIRREL1 ablation enhances hepatic YAP activity and hepatocyte reprogramming. Co-immunoprecipitation, CRISPR knockout, YAP activity reporter assays, in vivo mouse liver regeneration model Nature communications High 35177623
2022 KIRREL1 interacts with both SAV1 and LATS1/2, promoting LATS1/2 activation by MST1/2 Hippo kinases, thereby inhibiting YAP/TAZ oncoproteins. YAP/TAZ in turn transcriptionally induce KIRREL1 expression in a TEAD1-4-dependent manner, forming a negative feedback loop. Transgenic KIRREL1 expression blocks tumorigenesis in a mouse intrahepatic cholangiocarcinoma model. Co-immunoprecipitation, LATS1/2 kinase activity assays, transcriptional reporter assays, in vivo mouse tumor model Cell reports High 36044856
2022 In vivo CRISPR screen confirmed KIRREL1 loss promotes tumor growth; KIRREL1 directly binds SAV1 to activate the Hippo tumor suppressor pathway. In vivo CRISPR screen with custom cell surface protein library, Hippo pathway reporter screen, direct binding assays Proceedings of the National Academy of Sciences of the United States of America High 35704761
2024 Neph1 is required for neurite branching in developing spinal cord dorsal horn neurons; the homeodomain transcription factor PRRXL1 directly binds Neph1 intronic regions (by ChIP) and prevents premature Neph1 expression in superficial dorsal horn laminae. Chromatin immunoprecipitation (ChIP), Neph1 loss-of-function analysis, neurite branching morphometric assay, spatiotemporal expression analysis Neural development Medium 39049046
2025 Cryo-electron tomography of human kidney tissue resolves the near-native slit diaphragm architecture as a fishnet-like lattice; an atomic model based on the Nephrin-Neph1 heterodimer reveals ~9 nm spacing in humans, establishing the structural basis for the filtration sieve. Cryo-electron tomography of native human kidney tissue, atomic modeling based on Nephrin-Neph1 heterodimer bioRxivpreprint Medium bio_10.1101_2025.09.24.678239

Source papers

Stage 0 corpus · 34 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2001 Proteinuria and perinatal lethality in mice lacking NEPH1, a novel protein with homology to NEPHRIN. Molecular and cellular biology 336 11416156
2002 NEPH1 defines a novel family of podocin interacting proteins. FASEB journal : official publication of the Federation of American Societies for Experimental Biology 178 12424224
2003 Neph1 and nephrin interaction in the slit diaphragm is an important determinant of glomerular permeability. The Journal of clinical investigation 170 12865409
2003 Nephrin and Neph1 co-localize at the podocyte foot process intercellular junction and form cis hetero-oligomers. The Journal of biological chemistry 151 12646566
2009 Sns and Kirre, the Drosophila orthologs of Nephrin and Neph1, direct adhesion, fusion and formation of a slit diaphragm-like structure in insect nephrocytes. Development (Cambridge, England) 138 19515699
2003 Homodimerization and heterodimerization of the glomerular podocyte proteins nephrin and NEPH1. Journal of the American Society of Nephrology : JASN 135 12660326
2007 Neph1 cooperates with nephrin to transduce a signal that induces actin polymerization. Molecular and cellular biology 125 17923684
2011 Motor protein Myo1c is a podocyte protein that facilitates the transport of slit diaphragm protein Neph1 to the podocyte membrane. Molecular and cellular biology 76 21402783
2008 Ischemic injury to kidney induces glomerular podocyte effacement and dissociation of slit diaphragm proteins Neph1 and ZO-1. The Journal of biological chemistry 71 18922801
2008 Neph1, a component of the kidney slit diaphragm, is tyrosine-phosphorylated by the Src family tyrosine kinase and modulates intracellular signaling by binding to Grb2. The Journal of biological chemistry 67 18258597
2006 Neuronal expression and interaction with the synaptic protein CASK suggest a role for Neph1 and Neph2 in synaptogenesis. The Journal of comparative neurology 48 16874800
2008 Dissociation of NEPH1 from nephrin is involved in development of a rat model of focal segmental glomerulosclerosis. American journal of physiology. Renal physiology 45 18715943
2014 Slit diaphragm protein Neph1 and its signaling: a novel therapeutic target for protection of podocytes against glomerular injury. The Journal of biological chemistry 40 24554715
2010 Recognition of pre- and postsynaptic neurons via nephrin/NEPH1 homologs is a basis for the formation of the Drosophila retinotopic map. Development (Cambridge, England) 40 20724453
2022 Cell adhesion molecule KIRREL1 is a feedback regulator of Hippo signaling recruiting SAV1 to cell-cell contact sites. Nature communications 30 35177623
2022 Transmembrane protein KIRREL1 regulates Hippo signaling via a feedback loop and represents a therapeutic target in YAP/TAZ-active cancers. Cell reports 25 36044856
2019 Mutations in KIRREL1, a slit diaphragm component, cause steroid-resistant nephrotic syndrome. Kidney international 23 31472902
2011 Trans-interaction of nephrin and Neph1/Neph3 induces cell adhesion that associates with decreased tyrosine phosphorylation of nephrin. The Biochemical journal 23 21306299
2009 Neph1 regulates steady-state surface expression of Slo1 Ca(2+)-activated K(+) channels: different effects in embryonic neurons and podocytes. American journal of physiology. Cell physiology 22 19794150
2022 Integrated screens uncover a cell surface tumor suppressor gene KIRREL involved in Hippo pathway. Proceedings of the National Academy of Sciences of the United States of America 21 35704761
2017 Targeting Neph1 and ZO-1 protein-protein interaction in podocytes prevents podocyte injury and preserves glomerular filtration function. Scientific reports 21 28935902
2017 Interaction of CD80 with Neph1: a potential mechanism of podocyte injury. Clinical and experimental nephrology 21 29022109
2017 Loss of Kirrel family members alters glomerular structure and synapse numbers in the accessory olfactory bulb. Brain structure & function 14 28815295
2021 Molecular and structural basis of olfactory sensory neuron axon coalescence by Kirrel receptors. Cell reports 13 34731636
2012 Solution structure analysis of cytoplasmic domain of podocyte protein Neph1 using small/wide angle x-ray scattering (SWAXS). The Journal of biological chemistry 13 22262837
2021 Phosphorylation of slit diaphragm proteins NEPHRIN and NEPH1 upon binding of HGF promotes podocyte repair. The Journal of biological chemistry 11 34391780
2014 Angiotensin II type 1 receptor blockade ameliorates proteinuria in puromycin aminonucleoside nephropathy by inhibiting the reduction of NEPH1 and nephrin. Journal of nephrology 11 25298195
2014 Neph1 is reduced in primary focal segmental glomerulosclerosis, minimal change nephrotic syndrome, and corresponding experimental animal models of adriamycin-induced nephropathy and puromycin aminonucleoside nephrosis. Nephron extra 11 25404935
2016 Structural Analysis of the Myo1c and Neph1 Complex Provides Insight into the Intracellular Movement of Neph1. Molecular and cellular biology 9 27044863
2023 KIRREL promotes the proliferation of gastric cancer cells and angiogenesis through the PI3K/AKT/mTOR pathway. Journal of cellular and molecular medicine 8 37909722
2013 Identification and characterization of novel Kirrel isoform during myogenesis. Physiological reports 8 24303129
2026 Anti-nephrin, anti-podocin and anti-Kirrel1 antibodies: biological challenges and clinical implications. Nephrology, dialysis, transplantation : official publication of the European Dialysis and Transplant Association - European Renal Association 3 40815258
2017 KIRREL is differentially expressed in adipose tissue from 'fertil+' and 'fertil-' cows: in vitro role in ovary? Reproduction (Cambridge, England) 3 29170164
2024 Neph1 is required for neurite branching and is negatively regulated by the PRRXL1 homeodomain factor in the developing spinal cord dorsal horn. Neural development 0 39049046