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CXCR4  Protein, Antibody, ELISA Kit, cDNA Clone

CXCR4 Related Area

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    CXCR4 Related Protein, Antibody, cDNA Gene, and ELISA Kits

      CXCR4 Related Protein, Antibody, cDNA Gene, and ELISA Kits

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      CXCR4 Summary & Protein Information

      CXCR4 Related Information

      CXCR4 Background

      Subunit structure: Monomer. Can form dimers. Interacts with CD164. Interacts with HIV-1 surface protein gp120 and Tat. Interacts with ARRB2; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3. Interacts with ARRC; the interaction is dependent on the C-terminal phosphorylation of CXCR4 and modulates calcium mobilization. Interacts (via the cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the interaction, enhanced by CXCL12, ubiquitinates CXCR4 and leads to its degradation. Interacts with extracellular ubiquitin. Interacts with human cytomegalovirus/HHV-5 protein UL78. Interacts with DBN1; this interaction is enhanced by antigenic stimulation. Following LPS binding, may form a complex with GDF5, HSP90AA1 and HSPA8. {ECO:0000269|PubMed:10074122, ECO:0000269|PubMed:10644702, ECO:0000269|PubMed:10756055, ECO:0000269|PubMed:10825158, ECO:0000269|PubMed:11027346, ECO:0000269|PubMed:11276205, ECO:0000269|PubMed:12034737, ECO:0000269|PubMed:16725153, ECO:0000269|PubMed:17077324, ECO:0000269|PubMed:18799424, ECO:0000269|PubMed:18834145, ECO:0000269|PubMed:19116316, ECO:0000269|PubMed:20048153, ECO:0000269|PubMed:20215400, ECO:0000269|PubMed:20228059, ECO:0000269|PubMed:20505072, ECO:0000269|PubMed:20929726, ECO:0000269|PubMed:22496149, ECO:0000269|PubMed:9427609}.
      Domain: The amino-terminus is critical for ligand binding. Residues in all four extracellular regions contribute to HIV-1 coreceptor activity. {ECO:0000269|PubMed:10074122}.
      Subcellular location: Cell membrane; Multi-pass membrane protein. Cell junction. Early endosome. Late endosome. Lysosome. Note=In unstimulated cells, diffuse pattern on plasma membrane. On agonist stimulation, colocalizes with ITCH at the plasma membrane where it becomes ubiquitinated. In the presence of antigen, distributes to the immunological synapse forming at the T-cell-APC contact area, where it localizes at the peripheral and distal supramolecular activation cluster (SMAC).
      Tissue specificity: Expressed in numerous tissues, such as peripheral blood leukocytes, spleen, thymus, spinal cord, heart, placenta, lung, liver, skeletal muscle, kidney, pancreas, cerebellum, cerebral cortex and medulla (in microglia as well as in astrocytes), brain microvascular, coronary artery and umbilical cord endothelial cells. Isoform 1 is predominant in all tissues tested. {ECO:0000269|PubMed:11276205}.
      Post-translational: Phosphorylated on agonist stimulation. Rapidly phosphorylated on serine and threonine residues in the C-terminal. Phosphorylation at Ser-324 and Ser-325 leads to recruitment of ITCH, ubiquitination and protein degradation. {ECO:0000269|PubMed:14602072, ECO:0000269|PubMed:19116316, ECO:0000269|PubMed:20048153}.; Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The ubiquitin-dependent mechanism, endosomal sorting complex required for transport (ESCRT), then targets CXCR4 for lysosomal degradation. This process is dependent also on prior Ser-/Thr-phosphorylation in the C-terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S. {ECO:0000269|PubMed:14602072}.; Sulfation on Tyr-21 is required for efficient binding of CXCL12/SDF-1alpha and promotes its dimerization. Tyr-7 and Tyr-12 are sulfated in a sequential manner after Tyr-21 is almost fully sulfated, with the binding affinity for CXCL12/SDF-1alpha increasing with the number of sulfotyrosines present. Sulfotyrosines Tyr-7 and Tyr-12 occupy clefts on opposing CXCL12 subunits, thus bridging the CXCL12 dimer interface and promoting CXCL12 dimerization. {ECO:0000269|PubMed:10089882, ECO:0000269|PubMed:12034737, ECO:0000269|PubMed:16725153, ECO:0000269|PubMed:18834145}.; O- and N-glycosylated. Asn-11 is the principal site of N-glycosylation. There appears to be very little or no glycosylation on Asn-176. N-glycosylation masks coreceptor function in both X4 and R5 laboratory-adapted and primary HIV-1 strains through inhibiting interaction with their Env glycoproteins. The O-glycosylation chondroitin sulfate attachment does not affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity. {ECO:0000269|PubMed:10756055, ECO:0000269|PubMed:12034737}.
      Involvement in disease: DISEASE: WHIM syndrome (WHIM) [MIM:193670]: Immunodeficiency disease characterized by neutropenia, hypogammaglobulinemia and extensive human papillomavirus (HPV) infection. Despite the peripheral neutropenia, bone marrow aspirates from affected individuals contain abundant mature myeloid cells, a condition termed myelokathexis. Note=The disease is caused by mutations affecting the gene represented in this entry.
      Sequence similarity: Belongs to the G-protein coupled receptor 1 family. {ECO:0000255|PROSITE-ProRule:PRU00521}.
      General information above from UniProt

      CXCR4 Alternative Name

      b2b220Clo,CD184,Cmkar4,PB-CKR,PBSF/SDF-1, [Mouse]
      LESTR,Sdf1r,CD184,Cmkar4,PB-CKR,b2b220Clo,PBSF/SDF-1, [mus-musculus]

      CXCR4 Related Studies