| protein
| interacting with LDLRAP1 |
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interacting with Hepatitis C virus E1 and E2 proteins |
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interacting with PCSK9  |
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MYLIP-UBE2D complex is an important determinant of LDLR activity |
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PCSK9 binding to LDLR lead to its intracellular degradation instead of recycling back to cell membrane, and PCSK9-mediated LDLR degradation requires LDLR ubiquitination |
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LRP6 is indispensable for proper LDLR internalization |
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important role of FGF21 and CNPY2 in the regulation of LDLRs |
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PCSK9 is a secreted protein that promotes degradation of cell surface LDL receptors (LDLRs) in selected cell types |
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MYLIP is recruited to the plasma membrane by LDLR, promotes LDLR internalization in the absence of clathrin or caveolae, and facilitates LDLR degradation |
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MYLIP catalyzes the transfer of ubiquitin chains to itself and to the LDLR that do not contain exclusively K48 or K63 linkages |
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PCSK9 is capable of inducing degradation of LRP1, the latter is not an essential factor for LDLR regulation, but the LDLR effectively competes with LRP1 for PCSK9 activity |
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LDLR was shown to mediate clearance of blood coagulation factor VIII (F8) from the circulation |
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binding of WT- ectodomain (ED-LDLR) to pro-PCSK9 in the ER promotes autocatalytic cleavage of PCSK9, and autocatalytically cleaved PCSK9 acts as a chaperone to promote the exit of WT-ED-LDLR from the ER |
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interactors of GCGR, LDLR and TMED2, significantly enhanced glucagon-stimulated glucose production, while YWHAB inhibited glucose production |
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MYLIP is an E3 ubiquitin ligase that targets LDLR for degradation, is a critical determinant of brain APOE metabolism and APP plaque biogenesis |
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binding of PCSK9 to HSP90B1 protects LDLR from degradation likely by preventing early binding of PCSK9 to LDLR within the ER |
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PAQR3 plays a pivotal role in controlling hepatic LDLR degradation and blood LDL-C level via modulating LDLR-PCSK9 interaction |
