Fig 1: ZMYND10 interacts with a novel chaperone relay at a distinct stage of dynein heavy chain stability during cytoplasmic assembly.(A) Summary schematic of affinity purification-mass spectrometry (AP-MS) analysis of endogenous ZMYND10 interactomes from P30 mouse testes, overlapping between two commercial polyclonal Sigma (S) and Proteintech (P) antibodies. See also Supplementary file 2. (B) Endogenous ZMYND10 affinity purification with two validated ZMYND10 antibodies from Zmynd10 control and mutant P30 testes extracts confirm the ZMYND10 interaction with FKBP8 and HSP90AB1 (S only) in control samples. These interactions are not found in mutant samples lacking ZMYND10, serving as specificity controls. An in vivo interaction between ZMYND10 and LRRC6, as well as with DNAAF1, was not detected in reciprocal endogenous immunoprecipitations in P30 control testes extracts, using rIgG as a control. (C) Endogenous FKBP8 and DNAI1 immunoprecipitations in differentiating healthy human donor tracheal epithelial cultures (D17 ALI) both show binding of client DNAH5, the rest of the complexes are distinct, suggesting they act at sequential steps of assembly. (D) Endogenous ZMYND10 immunoprecipitation of client DNAH5 and chaperone HSP90, but not HSP70 from differentiating oviduct epithelial tissue (P7) using rIgG as a control. Protein molecular weights displayed in KDa.