The mitotic arrest deficient protein MAD2B interacts with the clathrin light chain A during mitosis

PloS One
Klaas MedendorpAd Geurts van Kessel

Abstract

Although the mitotic arrest deficient protein MAD2B (MAD2L2) is thought to inhibit the anaphase promoting complex (APC) by binding to CDC20 and/or CDH1 (FZR1), its exact role in cell cycle control still remains to be established. Using a yeast two-hybrid interaction trap we identified the human clathrin light chain A (CLTA) as a novel MAD2B binding protein. A direct interaction was established in mammalian cells via GST pull-down and endogenous co-immunoprecipitation during the G2/M phase of the cell cycle. Through subsequent confocal laser scanning microscopy we found that MAD2B and CLTA co-localize at the mitotic spindle. Clathrin forms a trimeric structure, i.e., the clathrin triskelion, consisting of three heavy chains (CLTC), each with an associated light chain. This clathrin structure has previously been shown to be required for the function of the mitotic spindle through stabilization of kinetochore fibers. Upon siRNA-mediated MAD2B depletion, we found that CLTA was no longer concentrated at the mitotic spindle but, instead, diffusely distributed throughout the cell. In addition, we found a marked increase in the percentage of misaligned chromosomes. Previously, we identified MAD2B as an interactor of the renal cell carc...Continue Reading

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Related Concepts

Pathologic Cytolysis
Establishment and Maintenance of Localization
Clathrin Complex
Immunofluorescence Assay
Tryptophan
Spindle
Benign Neoplasm of Testis
Galactosidase Activity
Inflammatory Myofibroblastic Tumor
Transfection

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