BioPAX pathway converted from "p62 recruits an atypical PKC" in the Reactome database. LEFT-TO-RIGHT p62 recruits an atypical PKC This event has been computationally inferred from an event that has been demonstrated in another species.<p>The inference is based on the homology mapping from PANTHER. Briefly, reactions for which all involved PhysicalEntities (in input, output and catalyst) have a mapped orthologue/paralogue (for complexes at least 75% of components must have a mapping) are inferred to the other species. High level events are also inferred for these events to allow for easier navigation.<p><a href='/electronic_inference_compara.html' target = 'NEW'>More details and caveats of the event inference in Reactome.</a> For details on PANTHER see also: <a href='http://www.pantherdb.org/about.jsp' target='NEW'>http://www.pantherdb.org/about.jsp</a> NGF ligand:p75NTR:Phospho-IRAK1:TRAF6:p62 Reactome DB_ID: 9832570 plasma membrane GENE ONTOLOGY GO:0005886 NGF ligand:p75NTR:Phospho-IRAK1:TRAF6 Reactome DB_ID: 9832568 Q62406 phospho-p-S,T-IRAK1 Reactome DB_ID: 9832566 cytosol GENE ONTOLOGY GO:0005829 UniProt:Q62406 Irak1 Irak1 Il1rak FUNCTION Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3 (By similarity).SUBUNIT Homodimer (By similarity). Forms a complex with TRAF6, PELI1, IRAK4 and MYD88 (PubMed:16951688). Direct binding of SMAD6 to PELI1 prevents complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression (By similarity). The TRAF6-PELI1-IRAK4-MYD88 complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation (By similarity). Interaction with MYD88 recruits IRAK1 to the stimulated receptor complex (By similarity). Interacts with TOLLIP; this interaction occurs in the cytosol prior to receptor activation (By similarity). Interacts with IL1RL1 (By similarity). Interacts (when polyubiquitinated) with IKBKG/NEMO (By similarity). Interacts with RSAD2/viperin (PubMed:21435586). Interacts with IRAK1BP1 (PubMed:11096118). Interacts with PELI2 (PubMed:12370331). Interacts with ZC3H12A; this interaction increases the interaction between ZC3H12A and IKBKB/IKKB (PubMed:22037600). Interacts with IRAK4 (By similarity). Interacts with PELI3 (By similarity). Interacts with PELI1 and TRAF6 (By similarity). Interacts with INAVA; the interaction takes place upon PRR stimulation (By similarity). Interacts (via C-terminus) with NFATC4 (via N-terminus) (By similarity).TISSUE SPECIFICITY Highly expressed in liver, followed by kidney and skeletal muscle.DEVELOPMENTAL STAGE Expressed from 11 dpc to 18 dpc.DOMAIN The ProST region is composed of many proline and serine residues (more than 20 of each) and some threonines. This region is the site of IRAK-1 hyperphosphorylation (By similarity).PTM Following recruitment on the activated receptor complex, phosphorylated on Thr-209, probably by IRAK4, resulting in a conformational change of the kinase domain, allowing further phosphorylations to take place. Thr-387 phosphorylation in the activation loop is required to achieve full enzymatic activity (By similarity).PTM Polyubiquitinated by TRAF6 after cell stimulation with IL-1-beta by PELI1, PELI2 and PELI3. Polyubiquitination occurs with polyubiquitin chains linked through 'Lys-63'. Ubiquitination promotes interaction with NEMO/IKBKG. Also sumoylated; leading to nuclear translocation (By similarity).DISRUPTION PHENOTYPE Mice show a loss in TLR7- and TLR9-mediated IFN-alpha production in plasmacytoid dendritic cells demonstrating an important role in innate immune response.SIMILARITY Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Pelle subfamily. Mus musculus NCBI Taxonomy 10090 UniProt Q62406 O-phospho-L-serine MOD MOD:00046 O-phospho-L-threonine MOD MOD:00047 1 EQUAL 712 EQUAL Reactome Database ID Release 82 9832566 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832566 Reactome R-MMU-3149574 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-3149574.1 Reactome http://www.reactome.org 1 Traf6 TRAF6 P70196 Reactome DB_ID: 9828388 UniProt:P70196 Traf6 Traf6 FUNCTION E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2 (PubMed:15322147, PubMed:17633018). Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation (By similarity). Leads to the activation of NF-kappa-B and JUN. Seems to also play a role in dendritic cells (DCs) maturation and/or activation (PubMed:14499111). Represses c-Myb-mediated transactivation, in B-lymphocytes (By similarity). Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor (PubMed:10421844, PubMed:10215628). Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation (PubMed:10421844, PubMed:17092936). Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (PubMed:12881420).PATHWAY Protein modification; protein ubiquitination.SUBUNIT Homotrimer (By similarity). Homooligomer (By similarity). N-terminal region is dimeric while C-terminal region is trimeric; maybe providing a mode of oligomerization. Upon IL1B treatment, forms a complex with PELI1, IRAK1, IRAK4 and MYD88; this complex recruits MAP3K7/TAK1, TAB1 and TAB2 to mediate NF-kappa-B activation. Direct binding of SMAD6 to PELI1 prevents the complex formation and hence negatively regulates IL1R-TLR signaling and eventually NF-kappa-B-mediated gene expression. Binds to TNFRSF5/CD40 and TNFRSF11A/RANK (By similarity). Associates with NGFR, TNFRSF17, IRAK2, IRAK3, PELI2, PELI3, RIPK2, MAP3K1, MAP3K5, MAP3K14, CSK, TRAF, TRAF-interacting protein TRIP and TNF receptor associated protein TDP2. Binds UBE2V1. Interacts with MAVS/IPS1. Interacts with TAX1BP1 (By similarity). Interacts with IL17R. Interacts with SQSTM1 bridging NTRK1 and NGFR. Forms a ternary complex with SQSTM1 and PRKCZ. Interacts with IL1RL1. Interacts with AJUBA (By similarity). Interacts with TRAFD1. Interacts with TICAM2. Interacts with ZFAND5. Interacts with ARRB1 and ARRB2 (By similarity). Interacts with MAP3K7 and TAB1/MAP3K7IP1; during IL-1 signaling. Interacts with UBE2N. Interacts with TGFBR1, HDAC1 and RANGAP1. Interacts with AKT1, AKT2 and AKT3. Interacts (via TRAF domains) with NUMBL (via C-terminal) (By similarity). Interacts (via TRAF domains) with DYNC2I2 (via WD domains). Interacts with RBCK1 (By similarity). Interacts with LIMD1 (via LIM domains). Interacts with RSAD2/viperin. Interacts with IFIT3 (via N-terminus) (By similarity). Interacts (via C-terminus) with EIF2AK2/PKR (via the kinase catalytic domain). Interacts with CARD14 (By similarity). Interacts with CD40 and MAP3K8; the interaction is required for ERK activation. Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1 (By similarity). Interacts with TANK; this interaction increases in response to DNA damage (By similarity). Interacts with USP10; this interaction increases in response to DNA damage (By similarity). Interacts with ZC3H12A; this interaction increases in response to DNA damage and is stimulated by TANK (By similarity). Interacts with WDFY3 (PubMed:27330028). Interacts with TRIM13 (By similarity). Interacts with GPS2 (PubMed:22424771). Interacts (via C-terminus) with SASH1 (By similarity). Interacts with LRRC19 (By similarity). Interacts with IL17RA AND TRAF3IP2. Interacts with TOMM70 (By similarity). Interacts with AMBRA1; interaction is required to mediate 'Lys-63'-linked ubiquitination of ULK1 (By similarity).TISSUE SPECIFICITY Highly expressed in brain, lung, liver, skeletal muscle, and kidney; lower expression in heart, spleen, and testis.DOMAIN The coiled coil domain mediates homo- and hetero-oligomerization.DOMAIN The MATH/TRAF domain binds to receptor cytoplasmic domains.PTM Sumoylated on Lys-124, Lys-142 and Lys-461 with SUMO1.PTM Polyubiquitinated on Lys-124 by TRAF3IP2; after cell stimulation with IL17A (By similarity). Polyubiquitinated; after cell stimulation with IL1B or TGFB. This ligand-induced cell stimulation leads to dimerization/oligomerization of TRAF6 molecules, followed by auto-ubiquitination which involves UBE2N and UBE2V1 and leads to TRAF6 activation. This 'Lys-63' site-specific poly-ubiquitination appears to be associated with the activation of signaling molecules. Endogenous autoubiquitination occurs only for the cytoplasmic form. Deubiquitinated by USP10 in a TANK-dependent manner, leading to the negative regulation of NF-kappa-B signaling upon DNA damage. LRRC19 induces 'Lys-63' ubiquitination (PubMed:25026888).DISRUPTION PHENOTYPE Abrogation of IL-1-induced activation of NF-kappa-B, MAPK8/JNK and MAPK14/p38. Animals appear normal at birth but become smaller after one week. Show runting, failure of tooth eruption and die after three weeks. Exhibit severe osteopetrosis, thymic atrophy, lymph node deficiency, splenomegaly, and have alopecia and lack sweat glands.SIMILARITY Belongs to the TNF receptor-associated factor family. A subfamily. UniProt P70196 1 EQUAL 522 EQUAL Reactome Database ID Release 82 9828388 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9828388 Reactome R-MMU-166366 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-166366.1 1 mature NGF homodimer:p75NTR Reactome DB_ID: 9832561 beta-NGF homodimer Reactome DB_ID: 198272 extracellular region GENE ONTOLOGY GO:0005576 beta-NGF Reactome DB_ID: 181839 UniProt:P01139 Ngf Ngf Ngfb FUNCTION Nerve growth factor is important for the development and maintenance of the sympathetic and sensory nervous systems (PubMed:20036257). Extracellular ligand for the NTRK1 and NGFR receptors, activates cellular signaling cascades to regulate neuronal proliferation, differentiation and survival (PubMed:22649032). The immature NGF precursor (proNGF) functions as ligand for the heterodimeric receptor formed by SORCS2 and NGFR, and activates cellular signaling cascades that lead to inactivation of RAC1 and/or RAC2, reorganization of the actin cytoskeleton and neuronal growth cone collapse (PubMed:22155786). In contrast to mature NGF, the precursor form (proNGF) promotes neuronal apoptosis (in vitro) (PubMed:20036257). Inhibits metalloproteinase-dependent proteolysis of platelet glycoprotein VI (By similarity). Binds lysophosphatidylinositol and lysophosphatidylserine between the two chains of the homodimer (PubMed:22649032, PubMed:26144237). The lipid-bound form promotes histamine relase from mast cells, contrary to the lipid-free form (PubMed:22649032).SUBUNIT Homodimer (PubMed:1956407, PubMed:8201620, PubMed:20036257, PubMed:22649032, PubMed:26144237, PubMed:30061605). The homodimer interacts with a single NTRK1 chain (PubMed:22649032). The homodimer interacts with a single NGFR chain (By similarity). The NGF dimer interacts with a single SORCS2 chain (via extracellular domain) (PubMed:30061605). The NGF precursor (proNGF) binds to a receptor complex formed by SORT1 and NGFR, which leads to NGF endocytosis (PubMed:20036257). Both mature NGF and the immature NGF precursor (proNGF) interact with SORCS2 and with the heterodimer formed by SORCS2 and NGFR (via extracellular domains) (PubMed:22155786, PubMed:30061605). The NGF precursor (proNGF) has much higher affinity for SORCS2 than mature NGF (PubMed:24908487). The NGF precursor (proNGF) has much higher affinity for SORT1 than mature NGF (PubMed:20036257). Interacts with ADAM10 in a divalent cation-dependent manner (By similarity).TISSUE SPECIFICITY Detected in submaxillary gland (at protein level) (PubMed:1284621). Highly expressed in male submaxillary gland. Levels are much lower in female submaxillary gland (PubMed:6336309, PubMed:1284621).INDUCTION Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain.SIMILARITY Belongs to the NGF-beta family. UniProt P01139 122 EQUAL 241 EQUAL Reactome Database ID Release 82 181839 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=181839 Reactome R-MMU-181839 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-181839.1 2 Reactome Database ID Release 82 198272 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=198272 Reactome R-MMU-198272 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-198272.1 1 Ngfr NGFR Q9Z0W1 Reactome DB_ID: 9832555 UniProt:Q9Z0W1 Ngfr Ngfr Tnfrsf16 FUNCTION Low affinity neurotrophin receptor which can bind to mature NGF, BDNF, NTF3, and NTF4 (PubMed:11559852, PubMed:1317267). Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF (proNGF), BDNF (proBDNF) and NTF3 (proNT3) with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:22155786, PubMed:24908487, PubMed:27457814). Plays an important role in differentiation and survival of specific neuronal populations during development (PubMed:1317267, PubMed:11559852). Can mediate cell survival as well as cell death of neural cells (PubMed:1317267, PubMed:11559852, PubMed:24908487). The heterodimeric receptor formed with SORCS2 plays a role in proBDNF-dependent synaptic plasticity, in hippocampal long term depression (LTD) and long term potentiation (LTP) (PubMed:27457814). Plays a role in the inactivation of RHOA (By similarity). Plays a role in the regulation of the translocation of GLUT4 to the cell surface in adipocytes and skeletal muscle cells in response to insulin, probably by regulating RAB31 activity, and thereby contributes to the regulation of insulin-dependent glucose uptake (PubMed:22460790). Necessary for the circadian oscillation of the clock genes ARNTL/BMAL1, PER1, PER2 and NR1D1 in the suprachiasmatic nucleus (SCN) of the brain and in liver and of the genes involved in glucose and lipid metabolism in the liver (PubMed:23785138).FUNCTION (Microbial infection) Cell surface receptor for rabies virus glycoprotein Gs.SUBUNIT Homodimer; disulfide-linked. Heterodimer with SORCS2 (PubMed:22155786, PubMed:24908487, PubMed:27457814). The extracellular domains of the heterodimer bind NGF. The cytoplasmic region of the heterodimer binds TRIO. NGF binding mediates dissociation of TRIO from the receptor complex (PubMed:22155786). Interacts with TRAF2, TRAF4, TRAF6, PTPN13 and RANBP9. Interacts through TRAF6 with SQSTM1 which bridges NGFR to NTRK1. Interacts with BEX1 (By similarity). Interacts with BEX3 (PubMed:11830582). Interacts with KIDINS220 and NTRK1. Can form a ternary complex with NTRK1 and KIDINS220 and this complex is affected by the expression levels of KIDINS220. An increase in KIDINS220 expression leads to a decreased association of NGFR and NTRK1. Interacts (via death domain) with RAB31 (PubMed:22460790). Interacts with NTRK2; may regulate the ligand specificity of the NTRK2 receptor (PubMed:11559852). Interacts with LINGO1. Interacts with NRADD. Interacts with MAGED1; the interaction antagonizes the association NGFR:NTRK1 (By similarity). Interacts with RTN4R (PubMed:22923615). Interacts (via death domain) with ARHGDIA and RIPK2 (By similarity).SUBUNIT (Microbial infection) Binds to rabies virus glycoprotein Gs.TISSUE SPECIFICITY Detected in Schwann cells (PubMed:11559852). Detected in embryonic brain, in hippocampus neurons (at protein level) (PubMed:22155786, PubMed:27457814). Detected in brain and spinal cord (PubMed:11559852).DEVELOPMENTAL STAGE Detected in embryonic large blood vessels at 11.5 dpc.INDUCTION Expression oscillates in a circadian manner in the suprachiasmatic nucleus (SCN) of the brain and in liver. Expression seen at higher levels during the light period and lower during the dark period.DOMAIN The death domain mediates interaction with RANBP9 (By similarity). It also mediates interaction with ARHGDIA and RIPK2 (By similarity).DOMAIN The extracellular domain is responsible for interaction with NTRK1.PTM N-glycosylated (PubMed:11559852). O-glycosylated.PTM Phosphorylated on serine residues.DISRUPTION PHENOTYPE Embryos are present at the expected Mendelian rate at 15.5 dpc, but mutant mice display about 40% perinatal lethality. At 11.5 dpc, mutant embryos display mildly to severely dilated blood vessels with thinner walls. The dorsal aorta is particularly affected. Many embryos show massive dilatations, ruptures and blood leakage. Surviving animals display small size and hind limb ataxia at 13 days after birth. When held by their tails, they respond by stretching their hind legs pointing upwards. The diameter of their sciatic nerve is strongly reduced. At 3 days after birth, the number of Schwann cells is strongly reduced in sciatic nerve from mutant mice. Likewise, the number of sensory neurons in dorsal root ganglia is strongly reduced (PubMed:11559852). The initially reported gene disruption experiment finds that mice are born at the expected Mendelian rate, are fertile, and have no visible phenotype when young. However, after 4 months mutant mice develop skin alterations with severe ulcers on all extremities. Already before the onset of symptoms, mutant mice display decreased skin innervation and smaller dorsal root ganglia, plus impaired heat sensitivity (PubMed:11559852).CAUTION The initial gene disruption experiment found a less pronounced phenotype than that reported in a later study (PubMed:1317267, PubMed:11559852). Both experiments disrupt expression of isoform 1 and NGF binding (PubMed:1317267, PubMed:11559852). The differences may be due to the presence of isoform 2; its expression is disrupted in the later experiment, but not in the initial experiment (PubMed:11559852). UniProt Q9Z0W1 29 EQUAL 427 EQUAL Reactome Database ID Release 82 9832555 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832555 Reactome R-MMU-193664 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-193664.1 1 Reactome Database ID Release 82 9832561 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832561 Reactome R-MMU-205123 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-205123.1 1 Reactome Database ID Release 82 9832568 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832568 Reactome R-MMU-209569 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-209569.1 1 SQSTM1 Q64337 Reactome DB_ID: 9832559 UniProt:Q64337 UniProt Q64337 1 EQUAL 440 EQUAL Reactome Database ID Release 82 9832559 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832559 Reactome R-MMU-193937 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-193937.1 1 Reactome Database ID Release 82 9832570 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832570 Reactome R-MMU-209577 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-209577.1 PRKCI Q62074 Reactome DB_ID: 9832669 UniProt:Q62074 UniProt Q62074 2 EQUAL 596 EQUAL Reactome Database ID Release 82 9832669 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832669 Reactome R-MMU-58206 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-58206.1 NGF ligand:p75NTR:Phospho-IRAK1:TRAF6:p62:aPKCi Reactome DB_ID: 9832671 1 1 Reactome Database ID Release 82 9832671 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832671 Reactome R-MMU-209558 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-209558.1 Reactome Database ID Release 82 9832673 Database identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser?DB=gk_current&ID=9832673 Reactome R-MMU-193684 1 Reactome stable identifier. Use this URL to connect to the web page of this instance in Reactome: http://www.reactome.org/cgi-bin/eventbrowser_st_id?ST_ID=R-MMU-193684.1 The atypical protein kinase C-iota isoform (aPKC-i) is recruited to the p75NTR receptor complex by p62 and becomes active. p62 recruits aPKC both via TRAF6 and RIP2. 11244088 Pubmed 2001 The atypical protein kinase C-interacting protein p62 is a scaffold for NF-kappaB activation by nerve growth factor Wooten, MW Seibenhener, ML Mamidipudi, V Diaz-Meco, MT Barker, PA Moscat, J J Biol Chem 276:7709-12 inferred from electronic annotation EVIDENCE CODE ECO:0000203