Ankyrin Repeats of ANKRA2 Recognize a PxLPxL Motif on the 3M Syndrome Protein CCDC8

SummaryPeptide motifs are often used for protein-protein interactions. We have recently demonstrated that ankyrin repeats of ANKRA2 and the paralogous bare lymphocyte syndrome transcription factor RFXANK recognize PxLPxL/I motifs shared by megalin, three histone deacetylases, and RFX5. We show here that that CCDC8 is a major partner of ANKRA2 but not RFXANK in cells. The CCDC8 gene is mutated in 3M syndrome, a short-stature disorder with additional facial and skeletal abnormalities. Two other genes mutated in this syndrome encode CUL7 and OBSL1. While CUL7 is a ubiquitin ligase and OBSL1 associates with the cytoskeleton, little is known about CCDC8. Binding and structural analyses reveal that the ankyrin repeats of ANKRA2 recognize a PxLPxL motif at the C-terminal region of CCDC8. The N-terminal part interacts with OBSL1 to form a CUL7 ligase complex. These results link ANKRA2 unexpectedly to 3M syndrome and suggest novel regulatory mechanisms for histone deacetylases and RFX7

Tree modules and counting polynomials

We give a formula for counting tree modules for the quiver S_g with g loops and one vertex in terms of tree modules on its universal cover. This formula, along with work of Helleloid and Rodriguez-Villegas, is used to show that the number of d-dimensional tree modules for S_g is polynomial in g with the same degree and leading coefficient as the counting polynomial A_{S_g}(d, q) for absolutely indecomposables over F_q, evaluated at q=1.Comment: 11 pages, comments welcomed, v2: improvements in exposition and some details added to last sectio