Daniel Capelluto

About

Daniel Capelluto is a Professor of Biological Sciences at Virginia Tech, located in the Department of Biological Sciences within the College of Science. His major field of interest includes the biochemistry and structural biology of protein-protein and protein-lipid interactions. His current research focuses on protein domains engaged in Wnt signaling, domains that control blood clotting, multimodular proteins that regulate inflammation processes, and lipid-binding proteins that mediate the entry of oomycetes into plant cells. He has an extensive academic background, including a Ph.D. in Chemical Sciences from the University of Buenos Aires, Argentina, with a thesis on serine hydroxymethyltransferase in Trypanosomatids. His postdoctoral work was conducted at the University of Colorado Health Sciences Center, where he specialized in structural and cell biology. Capelluto has held various academic positions at Virginia Tech, including Assistant Professor and Research Assistant Professor, and has also worked as an instructor at the University of Colorado. His research contributions are recognized through numerous awards, including the Biophysical Society Faculty Bridging Travel Funds Award, the Mary Louise Anderson Cancer Research Award, and the College of Science Diversity Award, among others. He is actively involved in research that advances understanding of protein interactions and cellular processes relevant to health and disease.

Research topics

• Biochemistry
• Computer Science
• Biology
• Chemistry
• Philosophy
• Stereochemistry
• Cell biology

Selected publications

• Protein Trafficking or Cell Signaling: A Dilemma for the Adaptor Protein TOM1

  Frontiers in Cell and Developmental Biology · 2021 · 29 citations

  Senior authorCorresponding

  its VHS and GAT domains. Several ESCRT proteins, including TOLLIP, Endofin, and Hrs, have been reported to form a complex with TOM1 at early endosomal membrane surfaces, which may potentiate the role of TOM1 in cargo sorting. More recently, it was found that TOM1 is involved in other physiological processes, including autophagy, immune responses, and neuroinflammation, which crosstalk with its endosomal cargo sorting function. Alteration of TOM1 function has emerged as a phosphoinositide-depende…

  PublisherOA PDFDOI

• The repertoire of protein-sulfatide interactions reveal distinct modes of sulfatide recognition

  Frontiers in Molecular Biosciences · 2022 · 11 citations

  1st authorCorresponding

  Sulfatide is an abundant glycosphingolipid in the mammalian nervous system, kidney, trachea, gastrointestinal tract, spleen, and pancreas and is found in low levels in other tissues. Sulfatide is characterized by the presence of a sulfate group in the hydrophilic galactose moiety, with isoforms differing in their sphingosine base and the length, unsaturation, and hydroxylation of their acyl chain. Sulfatide has been associated with a variety of cellular processes including immune responses, cell…

  PublisherOA PDFDOI

• Comparative Binding Affinity Analysis of Soybean Meal Bowman-Birk and Kunitz Trypsin Inhibitors in Interactions with Animal Serine Proteases

  ACS Food Science & Technology · 2023-08-08 · 9 citations

  articleOpen accessSenior authorCorresponding

  Raw soybeans are not suitable for consumption due to their high levels of anti-nutritional factors, such as trypsin inhibitors (TIs). The two main TIs in soybean, the Kunitz trypsin inhibitor (KTI) and the Bowman-Birk trypsin inhibitor (BBTI), were isolated to evaluate the impact of meal processing on their binding affinities for animal serine proteases. BBTI showed a ∼10-fold stronger affinity for trypsin compared to KTI, whereas KTI showed a ∼40-fold stronger affinity for chymotrypsin than BBT…

  PublisherDOI

• The C-terminal acidic motif of Phafin2 inhibits PH domain binding to phosphatidylinositol 3-phosphate

  Biochimica et Biophysica Acta (BBA) - Biomembranes · 2020 · 9 citations

  Senior authorCorresponding
  PublisherDOI

• Preferential phosphatidylinositol 5-phosphate binding contributes to a destabilization of the VHS domain structure of Tom1

  Scientific Reports · 2019-07-26 · 6 citations

  articleOpen accessSenior author

  Tom1 transports endosomal ubiquitinated proteins that are targeted for degradation in the lysosomal pathway. Infection of eukaryotic cells by Shigella flexneri boosts oxygen consumption and promotes the synthesis of phosphatidylinositol-5-phosphate (PtdIns5P), which triggers Tom1 translocation to signaling endosomes. Removing Tom1 from its cargo trafficking function hinders protein degradation in the host and, simultaneously, enables bacterial survival. Tom1 preferentially binds PtdIns5P via its…

  PublisherOA PDFDOI

Recent grants

• Revealing the regulatory mechanisms of endosomal cargo transporters

  NSF · $841k · 2024–2026

• Molecular mechanism of TIRAP membrane targeting

  NIH · $161k · 2014–2017

• NIH Grant R03HD065999

  NIH · $153k · 2013

Frequent coauthors

• Carla V. Finkielstein

  Biomedical Research Institute

  44 shared

• S. Y. Xiao

  20 shared

• Wen Xiong

  Hubei University of Arts and Science

  18 shared

• Tuoxian Tang

  Virginia Tech

  17 shared

• Jeffrey F. Ellena

  McCormick (United States)

  13 shared

• Xiaolin Zhao

  Northeast Normal University

  11 shared

• Geoffrey S. Armstrong

  University of Colorado Boulder

  9 shared

• Brett M. Tyler

  Oregon State University

  9 shared

Awards & honors

• Biophysical Society, Faculty Bridging Travel Funds Award (20…
• Mary Louise Anderson Cancer Research Award (2016)
• Scholar of the Week, Virginia Tech (2015)
• College of Science Diversity Award (2015)
• Favorite Faculty, Virginia Tech (2014)

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