Myristoylation and the post-translational acquisition of hydrophobicity by the membrane immunoglobulin heavy-chain polypeptide in B lymphocytes.
Membrane immunoglobulin heavy chain in pre-B and in B cells is initially synthesized as a relatively hydrophilic protein that is nonetheless stably anchored in the endoplasmic reticulum membrane. In B cells, but not in pre-B cells, the membrane immunoglobulin heavy chain is post-translationally converted to a relatively hydrophobic form that partitions into the oil phase when solubilized with the phase-separating detergent Triton X-114. Covalent myristoylation of the membrane and secretory forms of immunoglobulin heavy chains as well as of light chains was observed in B cells. Myristoylation of the membrane immunoglobulin heavy chain correlates with its transport to the cell surface and its post-translational conversion to a relatively hydrophobic form. This post-translational modification is hydroxylamine resistant and may be responsible for the assembly and transport of membrane immunoglobulin to the cell surface in B cells.
D000818:Animals; D001402:B-Lymphocytes / Q000276:immunology*; D002460:Cell Line; D007143:Immunoglobulin Heavy Chains / Q000235:genetics*; D007147:Immunoglobulin Light Chains / Q000235:genetics; D007148:Immunoglobulin mu-Chains / Q000235:genetics; D007700:Kinetics; D051379:Mice; D009227:Myristic Acids / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D007143:Immunoglobulin Heavy Chains; D007147:Immunoglobulin Light Chains; D007148:Immunoglobulin mu-Chains; D009227:Myristic Acids