More than Numbers: R&D-related Disclosure and Firm Performance.

This dissertation examines the relation between reported financial performance and qualitative disclosure in the research and development (R&D) disclosure setting. While the influence of performance on firms’ disclosure decisions is a fundamental issue in the accounting literature, prior studies generally focus on how performance relates to the disclosure of quantitative financial information that directly summarizes financial performance. However, a significant quantity of firms’ disclosure is not directly captured in the financial statements and is more qualitative in nature (e.g., narratives or text). Using a sample firms make R&D investments, I investigate whether reported earnings performance influences firms’ incentives to disclose qualitative R&D-related information. I hypothesize that as current earnings performance decreases, R&D firms’ incentives to provide more R&D-related disclosure increase because lower earnings performance is associated with less useful financial statements and higher information asymmetry. Based on a detailed analysis of R&D-related disclosures, I find, consistent with my hypothesis, that current earnings performance is negatively related to qualitative disclosure. I also find that this relation is more pronounced for firms that place more importance on R&D and for firms with higher outside monitoring. In addition, I examine whether the qualitative and quantitative disclosures of R&D firms relate differently to reported performance. While my main results suggest that reported earnings performance is negatively associated with R&D-related disclosure, I find that R&D firms’ decisions to provide earnings guidance, a more quantitative type of disclosure, are positively related to reported performance. These findings highlight the complexity of firms’ disclosure strategies and suggest that performance can influence different types of disclosures in different ways. Thus, these findings have important implications for future research that considers firms disclosure decisions.Ph.D.Business AdministrationUniversity of Michigan, Horace H. Rackham School of Graduate Studieshttp://deepblue.lib.umich.edu/bitstream/2027.42/89743/1/kmerkley_1.pd

Selective Recruitment of an E2∼Ubiquitin Complex by an E3 Ubiquitin Ligase*

Background: Rbx1/ROC1 is an E3 ligase adaptor protein that functions with the E2 enzyme CDC34

The Human Cdc34 Carboxyl Terminus Contains a Non-covalent Ubiquitin Binding Activity That Contributes to SCF-dependent Ubiquitination*

Cdc34 is an E2 ubiquitin-conjugating enzyme that functions in conjunction with SCF (Skp1·Cullin 1·F-box) E3 ubiquitin ligase to catalyze covalent attachment of polyubiquitin chains to a target protein. Here we identified direct interactions between the human Cdc34 C terminus and ubiquitin using NMR chemical shift perturbation assays. The ubiquitin binding activity was mapped to two separate Cdc34 C-terminal motifs (UBS1 and UBS2) that comprise residues 206–215 and 216–225, respectively. UBS1 and UBS2 bind to ubiquitin in the proximity of ubiquitin Lys48 and C-terminal tail, both of which are key sites for conjugation. When bound to ubiquitin in one orientation, the Cdc34 UBS1 aromatic residues (Phe206, Tyr207, Tyr210, and Tyr211) are probably positioned in the vicinity of ubiquitin C-terminal residue Val70. Replacement of UBS1 aromatic residues by glycine or of ubiquitin Val70 by alanine decreased UBS1-ubiquitin affinity interactions. UBS1 appeared to support the function of Cdc34 in vivo because human Cdc34(1–215) but not Cdc34(1–200) was able to complement the growth defect by yeast Cdc34 mutant strain. Finally, reconstituted IκBα ubiquitination analysis revealed a role for each adjacent pair of UBS1 aromatic residues (Phe206/Tyr207, Tyr210/Tyr211) in conjugation, with Tyr210 exhibiting the most pronounced catalytic function. Intriguingly, Cdc34 Tyr210 was required for the transfer of the donor ubiquitin to a receptor lysine on either IκBα or a ubiquitin in a manner that depended on the neddylated RING sub-complex of the SCF. Taken together, our results identified a new ubiquitin binding activity within the human Cdc34 C terminus that contributes to SCF-dependent ubiquitination