Susan Wente | |
---|---|
14th President of Wake Forest University | |
Assumed office July 1, 2021 | |
Preceded by | Nathan O. Hatch |
Provost of Vanderbilt University | |
In office July 2014 –June 2021 | |
Preceded by | Richard C. McCarty |
Succeeded by | C. Cybele Raver |
Personal details | |
Born | 1962 (age 61–62) |
Education | University of Iowa (BS) University of California,Berkeley (PhD) |
Susan Wente (born 1962) is an American cell biologist and academic administrator currently serving as the 14th President of Wake Forest University. From 2014 to 2021 she was Provost and Vice Chancellor for Academic Affairs at Vanderbilt University. [1] Between August 15,2019 and June 30,2020,she served as interim Chancellor at Vanderbilt. [2] [3]
Wente completed her undergraduate studies at the University of Iowa. She graduated in 1984 with a Bachelor of Science degree in Biochemistry,earning both High Distinction and Honors. Wente completed her graduate studies at the University of California,Berkeley. She graduated in 1988 with a Ph.D. in the Department of Biochemistry under the advisor Jamingus. Her dissertation was titled "Site-Directed Mutations Altering the Active Site and the Nucleotide-Binding Site of Aspartate Transcarbamoylase." [4]
During her time at the University of Iowa (1980 - 1984),Wente worked as a research technician under F. Jeffery Field in the Lipid Research Core Laboratory at the University of Iowa College of Medicine. She was a student research collaborator with Marshall Elzinga in the Department of Biology at the Brookhaven National Laboratory in Upton,New York. Wente also completed her undergraduate thesis studies under the direction of Alice B. Fulton in the Department of Biochemistry. She became a teaching assistant in the Department of Biochemistry while at the University of California,Berkeley. Wente taught a biochemistry laboratory course the summer after obtaining her Ph.D. Wente engaged in a molecular biology postdoctoral fellowship with Ora Rosen at the Memorial Sloan Kettering Cancer Center in New York City from 1988 - 1989. She then completed a postdoctoral fellowship with Günter Blobel at the Laboratory of Cell Biology at the Howard Hughes Medical Institute at Rockefeller University in New York City from 1989 - 1993. She received a Beckman Young Investigators Award in 1996. [5] [6]
Wente became an assistant professor of Cell Biology and Physiology at the Washington University School of Medicine in St. Louis,Missouri in 1993 and associate professor in 1998. [4] She began working at Vanderbilt in 2002 as the department chair and professor of cell and developmental biology. [7] In December 2008,she became an assistant vice chancellor for research at Vanderbilt. In 2009,she was promoted to associate vice chancellor for research and senior associate dean for biomedical sciences. She was named Vanderbilt's provost and vice chancellor for academic affairs in July 2014. [8] Wente was announced as the 14th and first female President of Wake Forest University on January 29,2021,and assumed office on July 1,2021. [9]
Wente serves on the editorial boards for the journals Advances in Biological Regulation,Current Opinion in Cell Biology and Nucleus. [10] [11] She previously served as an editor of Molecular and Cellular Biology (1999-2003) and associate editor of Molecular Biology of the Cell (2004-2009). [12] She previously served on the editorial board of Traffic (2004-2014) and Molecular and Cellular Biology (1999-2013).
Wente's current[ when? ] research focuses on the cell's adaptability to changing environmental conditions. She focuses on the exchange of large molecules between the nucleus and the cytoplasm. She focuses mostly on the border of this exchange,called the NPC. Wente's work targets three specific questions:
To view the cells and perform her studies,Wente uses yeast and fluorescent imaging. She studies these cells by examining interactions between the NPCs and its receptors for imported and exported material. She further studies the NPCs by observing its supporting proteins and determining the functions of these proteins. In doing so,she can test different hypotheses and figure out how these proteins could potentially malfunction and lead to various disease pathologies. [13]
Wente has been the recipient of numerous awards throughout her career. In 1984,she was awarded the Susan B. Hancher Award,recognizing her leadership as a senior at the University of Iowa and the Sanxay Prize,a token of promising graduate studies. In that same year,she was awarded the Hancher-Finkbine Medallion,the highest award bestowed by the University of Iowa for graduating seniors. Wente was also awarded Outstanding Graduate Student Instructor (1985-1986) by the University of California,Berkeley. From 1988 - 1990,she was awarded the New York State Health Research Council Postdoctoral Fellowship,and,from 1991 - 1993,the National Research Service Award Fellowship for Postdoctoral Study. [4] In 2011,Wente received the Women in Cell Biology (WICB) Senior Leadership Award from the American Society for Cell Biology (ASCB). [14] Wente was elected Fellow of the American Association for the Advancement of Science (AAAS) in 2011. [15]
Other honors and awards include:National Institutes of Health,General Medical Sciences –MERIT Award 2010-2020 Nashville Medical News –‘Women to Watch’Class of 2014 NIH MERIT Award,2010–present John H. Exton Award —For Research Leading to Innovative Biological Concepts,2008 Steven and Michele Kirsch Foundation,Kirsch Investigator Award,2001 - 2003 Beckman Foundation Young Investigator Award,1996 - 1998 American Cancer Society Junior Faculty Research Award,1996 - 1999 University of Iowa,Dewey B. Stuit Honors Award,1982 Iowa Forensic League Hugh F. Seabury Award,1980
Below is a list of selected publications of Wente's in chronological order. [16]
Wente discusses the export of mRNPs through NPCs and the different requirements for this to occur. The article discusses the different functional domains and receptors required for this transport to occur. It provides evidence that these factors directly affect FG domain function and mRNA export. [17]
Soluble inositides are studied as possible second eukaryotic messengers. It is discovered that these inositides play a role in gene expression at various levels. The article suggests that the cell produces these inositides in localized areas in order to create quick signals within the body. The article also contains information regarding the way the cell responds to changing environments caused by extracellular stimuli which affect gene expression. [18]
Wente and her colleagues discuss the overall function of the nuclear pore complex (NPC). They discuss that NPCs are the only known means of exchange for materials between the nucleus and cytoplasm. They discuss the different types of nucleus to cytoplasm transport. They conclude that proper NPC development is essential for physiological functioning,which if damaged,could cause improper cell division. The article focuses largely on the issues surrounding the topic of NPC assembly and functioning. [19]
Wente and her colleagues provide the first evidence that the Ran GTPase cycle is essential in order to build the nuclear pore complex (NPC). They identified the different necessities to assemble NPCs using genetic information from Saccharomyces cerevisiae. They introduced mutant Ran factors and found that it caused nucleoporins and a poremembrane protein to be mislocalized. This caused disturbances in the membrane,so they were able to conclude that Ran mediation is required for proper NPC assembly. [20]
This article was Wente's first publication as the sole author. She discusses how nuclear pore complexes (NPCs) are the location for the entrance and exit of the nucleus. She defines the transport machinery for movement within the cell and gives future direction that researchers may now examine the interactions between shuttling transport factors and the static pore complex. [21]
This article also focuses on the protein transport in and out of the nucleus. In this article,Wente and her colleagues discuss the vast number of signal types,receptors,and proteins and how this suggests that there are many pathways for entrance to and exit from the nucleus. The mechanism of nucleocytoplasmic transport is also explained. [22]
Wente and her colleagues investigated the enzyme aspartate transcarbamoylase and the amino acid residues that assist in making it a catalyst. They found that Lys-84 is essential in order for the enzyme to be catalyst and that replacement of any of this residue would cause the enzyme to essentially become inactive. [23]
The cell nucleus is a membrane-bound organelle found in eukaryotic cells. Eukaryotic cells usually have a single nucleus,but a few cell types,such as mammalian red blood cells,have no nuclei,and a few others including osteoclasts have many. The main structures making up the nucleus are the nuclear envelope,a double membrane that encloses the entire organelle and isolates its contents from the cellular cytoplasm;and the nuclear matrix,a network within the nucleus that adds mechanical support.
The endomembrane system is composed of the different membranes (endomembranes) that are suspended in the cytoplasm within a eukaryotic cell. These membranes divide the cell into functional and structural compartments,or organelles. In eukaryotes the organelles of the endomembrane system include:the nuclear membrane,the endoplasmic reticulum,the Golgi apparatus,lysosomes,vesicles,endosomes,and plasma (cell) membrane among others. The system is defined more accurately as the set of membranes that forms a single functional and developmental unit,either being connected directly,or exchanging material through vesicle transport. Importantly,the endomembrane system does not include the membranes of plastids or mitochondria,but might have evolved partially from the actions of the latter.
A nuclear pore is a channel as part of the nuclear pore complex (NPC),a large protein complex found in the nuclear envelope of eukaryotic cells. The nuclear envelope (NE) surrounds the cell nucleus containing DNA and facilitates the selective membrane transport of various molecules.
Protein targeting or protein sorting is the biological mechanism by which proteins are transported to their appropriate destinations within or outside the cell. Proteins can be targeted to the inner space of an organelle,different intracellular membranes,the plasma membrane,or to the exterior of the cell via secretion. Information contained in the protein itself directs this delivery process. Correct sorting is crucial for the cell;errors or dysfunction in sorting have been linked to multiple diseases.
Telophase is the final stage in both meiosis and mitosis in a eukaryotic cell. During telophase,the effects of prophase and prometaphase are reversed. As chromosomes reach the cell poles,a nuclear envelope is re-assembled around each set of chromatids,the nucleoli reappear,and chromosomes begin to decondense back into the expanded chromatin that is present during interphase. The mitotic spindle is disassembled and remaining spindle microtubules are depolymerized. Telophase accounts for approximately 2% of the cell cycle's duration.
A nuclear localization signalorsequence (NLS) is an amino acid sequence that 'tags' a protein for import into the cell nucleus by nuclear transport. Typically,this signal consists of one or more short sequences of positively charged lysines or arginines exposed on the protein surface. Different nuclear localized proteins may share the same NLS. An NLS has the opposite function of a nuclear export signal (NES),which targets proteins out of the nucleus.
The intermembrane space (IMS) is the space occurring between or involving two or more membranes. In cell biology,it is most commonly described as the region between the inner membrane and the outer membrane of a mitochondrion or a chloroplast. It also refers to the space between the inner and outer nuclear membranes of the nuclear envelope,but is often called the perinuclear space. The IMS of mitochondria plays a crucial role in coordinating a variety of cellular activities,such as regulation of respiration and metabolic functions. Unlike the IMS of the mitochondria,the IMS of the chloroplast does not seem to have any obvious function.
Peter Walter is a German-American molecular biologist and biochemist. He is currently the Director of the Bay Area Institute of Science at Altos Labs and an emeritus professor at the Department of Biochemistry and Biophysics of the University of California,San Francisco (UCSF). He was a Howard Hughes Medical Institute (HHMI) Investigator until 2022.
Importin is a type of karyopherin that transports protein molecules from the cell's cytoplasm to the nucleus. It does so by binding to specific recognition sequences,called nuclear localization sequences (NLS).
An alpha solenoid is a protein fold composed of repeating alpha helix subunits,commonly helix-turn-helix motifs,arranged in antiparallel fashion to form a superhelix. Alpha solenoids are known for their flexibility and plasticity. Like beta propellers,alpha solenoids are a form of solenoid protein domain commonly found in the proteins comprising the nuclear pore complex. They are also common in membrane coat proteins known as coatomers,such as clathrin,and in regulatory proteins that form extensive protein-protein interactions with their binding partners. Examples of alpha solenoid structures binding RNA and lipids have also been described.
Nuclear transport refers to the mechanisms by which molecules move across the nuclear membrane of a cell. The entry and exit of large molecules from the cell nucleus is tightly controlled by the nuclear pore complexes (NPCs). Although small molecules can enter the nucleus without regulation,macromolecules such as RNA and proteins require association with transport factors known as nuclear transport receptors,like karyopherins called importins to enter the nucleus and exportins to exit.
The nuclear envelope,also known as the nuclear membrane,is made up of two lipid bilayer membranes that in eukaryotic cells surround the nucleus,which encloses the genetic material.
Nucleoporins are a family of proteins which are the constituent building blocks of the nuclear pore complex (NPC). The nuclear pore complex is a massive structure embedded in the nuclear envelope at sites where the inner and outer nuclear membranes fuse,forming a gateway that regulates the flow of macromolecules between the cell nucleus and the cytoplasm. Nuclear pores enable the passive and facilitated transport of molecules across the nuclear envelope. Nucleoporins,a family of around 30 proteins,are the main components of the nuclear pore complex in eukaryotic cells. Nucleoporin 62 is the most abundant member of this family. Nucleoporins are able to transport molecules across the nuclear envelope at a very high rate. A single NPC is able to transport 60,000 protein molecules across the nuclear envelope every minute.
Nucleoporin 107 (Nup107) is a protein that in humans is encoded by the NUP107 gene.
Nuclear pore complex protein Nup133,or Nucleoporin Nup133,is a protein that in humans is encoded by the NUP133 gene.
Nucleoporin 85 (Nup85) is a protein that in humans is encoded by the NUP85 gene.
Nucleoporin 155 (Nup155) is a protein that in humans is encoded by the NUP155 gene.
Inner nuclear membrane proteins are membrane proteins that are embedded in or associated with the inner membrane of the nuclear envelope. There are about 60 INM proteins,most of which are poorly characterized with respect to structure and function. Among the few well-characterized INM proteins are lamin B receptor (LBR),lamina-associated polypeptide 1 (LAP1),lamina-associated polypeptide-2 (LAP2),emerin and MAN1.
Gene gating is a phenomenon by which transcriptionally active genes are brought next to nuclear pore complexes (NPCs) so that nascent transcripts can quickly form mature mRNA associated with export factors. Gene gating was first hypothesised by Günter Blobel in 1985. It has been shown to occur in Saccharomyces cerevisiae,Caenorhabditis elegans,Drosophila melanogaster as well as mammalian model systems.
Mary C. Dasso is an American biochemist known for research on chromosome segregation and the discovery of Ran GTPase. She is the acting scientific director of the division of intramural research and a senior investigator in the section on cell cycle regulation at the Eunice Kennedy Shriver National Institute of Child Health and Human Development.