Maria Enquist-Newman

ExxonMobil (United States)

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David O. Morgan

University of California, San Francisco

Takahiro Matsusaka

Horizon Discovery Group (United Kingdom)

David G. Drubin

University of California, Berkeley

Iain M. Cheeseman

Whitehead Institute for Biomedical Research

Jonathon Pines

Institute of Cancer Research

Georjana Barnes

University of California, Berkeley

Li‐Mei Chang

Fuzhou University

Drew D. Regitsky

Manus Bio (United States)

Pramila Tamrakar

Novartis (United States)

Nicholas Ohler

University of California, Berkeley

Cooperative Institutions

University of California, Berkeley

ExxonMobil (United States)

University of California, San Francisco

University of Calgary

Manus Bio (United States)

Sutro Biopharma (United States)

Adamas Pharmaceuticals (United States)

Lawrence Berkeley National Laboratory

Stanford University

Willow Biosciences (Canada)

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The APC Subunit Doc1 Promotes Recognition of the Substrate Destruction Box

Current Biology (2005)

Christopher W. Carroll Maria Enquist-Newman David O. Morgan

Anaphase-promoting complex

Ubiquitin-Protein Ligases

CDC20

F-box protein

10.1016/j.cub.2004.12.066

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Citations (124)

Dad1p, Third Component of the Duo1p/Dam1p Complex Involved in Kinetochore Function and Mitotic Spindle Integrity

Molecular Biology of the Cell (2001)

Maria Enquist-Newman Iain M. Cheeseman David Van Goor David G. Drubin Pamela B. Meluh

We showed recently that a complex between Duo1p and Dam1p is required for both spindle integrity and kinetochore function in the budding yeast Saccharomyces cerevisiae. To extend our understanding of the functions and interactions of the Duo1p/Dam1p complex, we analyzed the novel gene product Dad1p (for Duo1 and Dam1 interacting). Dad1p physically associates with Duo1p by two-hybrid analysis, coimmunoprecipitates with Duo1p and Dam1p out of yeast protein extracts, and shows interdependent localization with Duo1p and Dam1p to the mitotic spindle. These results indicate that Dad1p functions as a component of the Duo1p/Dam1p complex. Like Duo1p and Dam1p, Dad1p also localizes to kinetochore regions in chromosomes spreads. Here, we also demonstrate by chromatin immunoprecipitation that Duo1p, Dam1p, and Dad1p associate specifically with centromeric DNA in a manner that is dependent upon Ndc10 and partially dependent upon the presence of microtubules. To explore the functions of Dad1p in vivo, we generated a temperature-sensitive allele, dad1-1. This allele shows spindle defects and a mitotic arrest phenotype that is dependent upon the spindle assembly checkpoint. In addition, dad1-1 mutants undergo chromosome mis-segregation at the restrictive temperature, resulting in a dramatic decrease in viability.

Spindle pole body

Mitotic exit

Spindle checkpoint

10.1091/mbc.12.9.2601

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Citations (62)

Co-activator independent differences in how the metaphase and anaphase APC/C recognise the same substrate

Biology Open (2014)

Takahiro Matsusaka Maria Enquist-Newman David O. Morgan Jonathon Pines

ABSTRACT The Anaphase Promoting Complex or Cyclosome (APC/C) is critical to the control of mitosis. The APC/C is an ubiquitin ligase that targets specific mitotic regulators for proteolysis at distinct times in mitosis, but how this is achieved is not well understood. We have addressed this question by determining whether the same substrate, cyclin B1, is recognised in the same way by the APC/C at different times in mitosis. Unexpectedly, we find that distinct but overlapping motifs in cyclin B1 are recognised by the APC/C in metaphase compared with anaphase, and this does not depend on the exchange of Cdc20 for Cdh1. Thus, changes in APC/C substrate specificity in mitosis can potentially be conferred by altering interaction sites in addition to exchanging Cdc20 for Cdh1.

CDC20

Anaphase-promoting complex

Mitotic exit

Cyclin B1

Cyclin A

Cyclin B

10.1242/bio.20149415

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Citations (10)

Mitotic Spindle Integrity and Kinetochore Function Linked by the Duo1p/Dam1p Complex

The Journal of Cell Biology (2001)

Iain M. Cheeseman Maria Enquist-Newman Thomas Müller‐Reichert David G. Drubin Georjana Barnes

Duo1p and Dam1p were previously identified as spindle proteins in the budding yeast, Saccharomyces cerevisiae. Here, analyses of a diverse collection of duo1 and dam1 alleles were used to develop a deeper understanding of the functions and interactions of Duo1p and Dam1p. Based on the similarity of mutant phenotypes, genetic interactions between duo1 and dam1 alleles, interdependent localization to the mitotic spindle, and Duo1p/Dam1p coimmunoprecipitation from yeast protein extracts, these analyses indicated that Duo1p and Dam1p perform a shared function in vivo as components of a protein complex. Duo1p and Dam1p are not required to assemble bipolar spindles, but they are required to maintain metaphase and anaphase spindle integrity. Immunofluorescence and electron microscopy of duo1 and dam1 mutant spindles revealed a diverse variety of spindle defects. Our results also indicate a second, previously unidentified, role for the Duo1p/Dam1p complex. duo1 and dam1 mutants show high rates of chromosome missegregation, premature anaphase events while arrested in metaphase, and genetic interactions with a subset of kinetochore components consistent with a role in kinetochore function. In addition, Duo1p and Dam1p localize to kinetochores in chromosome spreads, suggesting that this complex may serve as a link between the kinetochore and the mitotic spindle.

Spindle pole body

Spindle checkpoint

Mitotic exit

10.1083/jcb.152.1.197

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Citations (147)

A pathogenesis-related 10 protein catalyzes the final step in thebaine biosynthesis

Nature Chemical Biology (2018)

Chen Xue Jillian M. Hagel Li‐Mei Chang Joseph E. Tucker Stacey A. Shiigi

Thebaine

Opium Poppy

Poppy

10.1038/s41589-018-0059-7

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Citations (86)

Efficient ethanol production from brown macroalgae sugars by a synthetic yeast platform

Nature (2013)

Maria Enquist-Newman Ann Marie E. Faust Daniel D. Bravo Christine Nicole S. Santos Ryan Raisner

Metabolic Engineering

10.1038/nature12771

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Citations (323)

Regulation of the Anaphase-Promoting Complex in Late Mitosis

Maria Enquist-Newman

Author(s): Enquist-Newman, Maria | Advisor(s): Morgan, David O | Abstract: Polyubiquitination is an important mechanism by which proteins in all cellular processes are targeted for destruction. To understand this process we wanted to identify proteins in budding yeast that perform it, using an in vitro system to follow activities that add ubiquitin chains to a substrate that had already been modified by monoubiquitination. We detected a strong polyubiquitinating activity in yeast lysates. Initially we attempted to fractionate the lysates, but ultimately we identified the protein responsible for this strong polyubiquitinating activity using a candidate approach. It is the HECT-domain containing protein-ubiquitin ligase Tom1 that causes the large modification to the substrate in our in vitro assays. Tom1 appears to be a general polyubiquitinating activity in the cell, and as it is conserved all the way up to humans, it may be a general activity in all eukaryotic systems. The Anaphase-Promoting Complex (APC) is a protein-ubiquitin ligase that targets cell cycle proteins for destruction. It is a tightly regulated enzyme which needs to be associated with one of two activating subunits (Cdc20 or Cdh1) to be active. The ability of Cdh1 to bind and therefore activate the APC is regulated through phosphorylation by Cyclin-Dependent Kinase (CDK). An additional level of regulation is through binding of the protein inhibitor Acm1. Our studies show that on a molecular level, Acm1 is a specific inhibitor of APCCdh1, and has no affect on the activity of APCCdc20. Further, we showed that the inhibitory activity is dependent on a central region of Acm1 that contains motifs similar to the recognition motifs in APC-substrates. We also showed that Acm1 binds very tightly to Cdh1 independently of the inhibition region, with a Kd likely in the nano-molar range. Next we addressed the regulation of Acm1. The protein levels fluctuate through the cell cycle, and we showed that the destruction of Acm1 is mediated by APCCdc20. Moreover, we showed that Acm1 is phosphorylated by CDK and that this phosphorylation affects the localization and stability of Acm1.

CDC20

Anaphase-promoting complex

Mitotic exit

Ubiquitin-conjugating enzyme

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Co-activator independent differences in how the metaphase and anaphase APC/C recognise the same substrate - eScholarship

David O. Morgan Takahiro Matsusaka Maria Enquist-Newman D. F. Morgan Jonathon Pines

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