Cytosolic interaction of type III human CD38 with CIB1 modulates cellular cyclic ADP-ribose levels.

ABSTRACT: CD38 catalyzes the synthesis of the Ca²⁺ messenger, cyclic ADP-ribose (cADPR). It is generally considered to be a type II protein with the catalytic domain facing outside. How it can catalyze the synthesis of intracellular cADPR that targets the endoplasmic Ca²⁺ stores has not been resolved. We have proposed that CD38 can also exist in an opposite type III orientation with its catalytic domain facing the cytosol. Here, we developed a method using specific nanobodies to immunotarget two different epitopes simultaneously on the catalytic domain of the type III CD38 and firmly established that it is naturally occurring in human multiple myeloma cells. Because type III CD38 is topologically amenable to cytosolic regulation, we used yeast-two-hybrid screening to identify c

SUBMITTER: Liu J 

PROVIDER: S-EPMC5547619 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature