MYLIP
Developmental stage
Expressed in fetal tissues and higher levels were detected in placenta and fetal lung.
Domain
The RING domain mediates ubiquitination and the neurite outgrowth inhibitory activity.
The FERM domain binds phospholipids and mediates lipoprotein receptors recognition at the plasma membrane through their cytoplasmic tails.
The RING-type zinc finger mediates the interaction with UBE2D E2 enzymes.
Function
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Activity depends on E2 enzymes of the UBE2D family. Proteasomal degradation of MRLC leads to inhibit neurite outgrowth in presence of NGF by counteracting the stabilization of MRLC by saposin-like protein (CNPY2/MSAP) and reducing CNPY2-stimulated neurite outgrowth. Acts as a sterol-dependent inhibitor of cellular cholesterol uptake by mediating ubiquitination and subsequent degradation of LDLR.
Pathway
Protein modification; protein ubiquitination.
Post-translational modifications
Autoubiquitinated.
Tissue Specificity
Ubiquitously expressed.
Cellular localization
- Cytoplasm
- Cell membrane
- Peripheral membrane protein
Alternative names
BZF1, IDOL, BM-023, PP5242, MYLIP, E3 ubiquitin-protein ligase MYLIP, Inducible degrader of the LDL-receptor, Myosin regulatory light chain interacting protein, RING-type E3 ubiquitin transferase MYLIP, Idol, MIR