IFT46 and IFT52 are important for IFT B protein stability, while IFT88 is not.

<p>Western blot analysis of whole cell extracts of untreated strains or strains treated with cycloheximide. Coomassie-stained gels (in blue color) were used to show equal protein loadings. (A) <i>Bld1</i>, <i>ift46</i>, and <i>ift88</i> have different levels of reduction of IFT B proteins, and an increase or no change in IFT A proteins; <i>Bld1</i> shows the most extreme change, while <i>ift88</i> shows the least extreme change compared to wildtlype. (B–E) Cells were treated with cycloheximide, a protein synthesis inhibitor, to measure degradation rates of existing proteins within 16 hours of treatment. (B) In wild type (<i>cc125</i>) IFT A and IFT B proteins remain stable throughout the time course. (C) <i>Ift88</i> has near wild type stabilities of IFT A and IFT B proteins. (D) <i>Ift46</i> has stabilities much like <i>bld1</i> for IFT A and IFT B proteins. (E) <i>Bld1</i> has an extreme decrease in IFT B protein stabilities, with the exception of IFT25, and no change in stability of IFT A proteins.