DUB-1, a fate determinant of dynein heavy chain in B-lymphocytes, is regulated by the ubiquitin-proteasome pathway.

Ubiquitination and deubiquitination of post-translational modification play counter roles in determining the fate of protein function in eukaryotic system for maintaining the cellular homeostasis. Even though novel family members of growth-regulating deubiquitinating enzymes (DUB-1 and DUB-2) have been identified, their target proteins and functions are poorly understood. Dub genes encoding DUB-1 and DUB-2 are immediate-early genes and are induced in response to cytokine stimuli rapidly and transiently. In order to explore the possible proteins regulated by DUB-1, we performed the matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis followed by immunoprecipitation. We confirmed that DUB-1 interacts with dynein heavy chain, which is known to regulate the movement of organelles and microtubule binding ability. In addition, structural and immunoprecipitation analyses revealed that DUB-1 contains a putative PEST motif and is polyubiquitinated, indicating that DUB-1 is also regulated by the ubiquitin-proteasome pathway.

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