Upload your resume. PhdFit's six research agents compare your background with faculty profiles, recent publications, lab focus, and outreach opportunities, then rank professors with evidence you can review.
Ask how her lab is extending interpretability methods into fairness audits for real-world AI systems.
University of Pennsylvania · Biological Sciences
Active 1980–2026
Tatyana Svitkina is a Professor of Biology at the University of Pennsylvania. Her research interests focus on Cell and Developmental Biology. She is involved in exploring the mechanisms underlying cellular processes and developmental biology, contributing to the understanding of cell structure and function.
Current Biology · 2026-02-01
Author response: CCDC32 stabilizes clathrin-coated pits and drives their invagination
2026-01-05
Live cell imaging and biochemical analyses reveal that CCDC32 interacts with AP2 to stabilize and drive invagination of clathrin-coated pits, and that clinical mutations disrupting this interaction cause cardio-facio-neuro-developmental syndrome.
CCDC32 stabilizes clathrin-coated pits and drives their invagination
eLife · 2026-01-05 · 1 citations
Clathrin-mediated endocytosis (CME) is essential for maintaining homeostasis in mammalian cells. Previous studies have reported more than 50 CME accessory proteins; however, the mechanism driving the invagination of clathrin-coated pits (CCPs) remains elusive. We show by quantitative live cell imaging that siRNA-mediated knockdown of CCDC32, a poorly characterized endocytic accessory protein, leads to the accumulation of unstable flat clathrin assemblies. CCDC32 interacts with the α-appendage domain (AD) of AP2 in vitro and with full-length AP2 complexes in cells. Deletion of aa78-98 in CCDC32, corresponding to a predicted α-helix, abrogates AP2 binding and CCDC32’s early function in CME. Furthermore, clinically observed nonsense mutations in CCDC32, which result in C-terminal truncations that lack aa78-98, are linked to the development of cardio-facio-neuro-developmental syndrome (CFNDS). Overall, our data demonstrate the function of a novel endocytic accessory protein, CCDC32, in regulating CCP stabilization and invagination, critical early stages of CME.
Motor activity of nonmuscle myosin 2A is a key component of bipolar filament turnover in cells
bioRxiv (Cold Spring Harbor Laboratory) · 2026-03-11
ABSTRACT Cell contractility plays numerous essential roles in a healthy organism, while its malfunctioning can lead to disease. The ubiquitous actin-dependent motors of the nonmuscle myosin 2 (NM2) family, which includes NM2A and NM2B, are chiefly responsible for cell contractility because of their ability to polymerize into bipolar filaments. Polymerization/depolymerization of NM2 filaments allows cells to quickly reorganize their contractile system according to constantly changing shapes and positions of nonmuscle cells. Bipolar filament depolymerization is known to depend on the C-terminal features of the NM2A heavy chain. Here, we show that the motor activity of NM2A is another key component of NM2A’s depolymerization mechanism, which cooperates with tail-dependent mechanisms to facilitate NM2A turnover in cells and, through copolymerization with NM2B, to reorganize and dynamize NM2B in trans, thus generating a proper intracellular NM2A/NM2B distribution needed for efficient cell migration. Together, we show that NM2A motor activity is a key component of the bipolar filament depolymerization mechanism.
CCDC32 stabilizes clathrin-coated pits and drives their invagination
eLife · 2025-06-11
Clathrin-mediated endocytosis (CME) is essential for maintaining homeostasis in mammalian cells. Previous studies have reported more than 50 CME accessory proteins; however, the mechanism driving the invagination of clathrin-coated pits (CCPs) remains elusive. We show by quantitative live cell imaging that siRNA-mediated knockdown of CCDC32, a poorly characterized endocytic accessory protein, leads to the accumulation of unstable flat clathrin assemblies. CCDC32 interacts with the α-appendage domain (AD) of AP2 in vitro and with full-length AP2 complexes in cells. Deletion of aa78-98 in CCDC32, corresponding to a predicted α-helix, abrogates AP2 binding and CCDC32's early function in CME. Furthermore, clinically observed nonsense mutations in CCDC32, which result in C-terminal truncations that lack aa78-98, are linked to the development of cardio-facio-neuro-developmental syndrome (CFNDS). Overall, our data demonstrate the function of a novel endocytic accessory protein, CCDC32, in regulating CCP stabilization and invagination, critical early stages of CME.
Nonmuscle myosin 2 turnover in cells is synergistically controlled by the tail and the motor domain
bioRxiv (Cold Spring Harbor Laboratory) · 2025-05-02 · 1 citations
Myosin 2, an actin-dependent motor, is universally responsible for cell contractility due to its ability to form bipolar filaments. Fast turnover of nonmuscle myosin 2 (NM2) filaments is necessary to keep up with cell motility and shape changes. The turnover mechanisms are not fully understood and differ for two main mammalian paralogs-NM2A and NM2B-whereas paralog copolymerization adds complexity to this process by enabling the intrinsically fast NM2A to dynamize the intrinsically slow NM2B. Here, we show that the nonhelical tail, the C-terminal phosphorylation sites, and surprisingly, the motor domain of the NM2A heavy chain synergistically accelerate the turnover of NM2B in trans and cell motility, suggesting that these three mechanisms collectively control NM2A's own dynamics. Conversely, the phosphomimetic NM2B tail facilitates only local turnover of endogenous wild type NM2B but not its global redistribution unless the NM2A motor is combined with the phosphomimetic NM2B tail. Collectively, we reveal the cooperation between the motor activity and the NM2 tail-targeting turnover mechanisms in regulating the NM2 filament turnover in trans and cell motility. SUMMARY: Turnover of nonmuscle myosin 2 (NM2) filaments is essential for cell motility and is regulated by various mechanisms including copolymerization of the NM2A and NM2B paralogs. Chougule and Svitkina reveal how the intrinsically fast NM2A accelerates dynamics of slower NM2B in trans.
Author response: CCDC32 stabilizes clathrin-coated pits and drives their invagination
2025-08-15
Clathrin-mediated endocytosis (CME) is essential for maintaining cellular homeostasis. Previous studies have reported more than 50 CME accessory proteins; however, the mechanism driving the invagination of clathrin-coated pits (CCPs) remains elusive. We show by quantitative live cell imaging that siRNA-mediated knockdown of CCDC32, a poorly characterized endocytic accessory protein, leads to the accumulation of unstable flat clathrin assemblies. CCDC32 interacts with the α-appendage domain (AD) of AP2 in vitro and with full length AP2 complexes in cells. Deletion of aa78-98 in CCDC32, corresponding to a predicted α-helix, abrogates AP2 binding and CCDC32’s early function in CME. Furthermore, clinically observed nonsense mutations in CCDC32, which result in C-terminal truncations that lack aa78-98, are linked to the development of cardio-facio-neuro-developmental syndrome (CFNDS). Overall, our data demonstrate the function of a novel endocytic accessory protein, CCDC32, in regulating CCP stabilization and invagination, critical early stages of CME.We show that CCDC32, a poorly studied and functionally ambiguous protein, binds to AP2 and regulates CCP stabilization and invagination. Clinically observed mutations in CCDC32 lose their ability to interact with AP2 likely contributing to the development of cardio-facio-neuro-developmental syndrome.
Author Reply to Peer Reviews of CCDC32 stabilizes clathrin-coated pits and drives their invagination
2025-01-21
CCDC32 stabilizes clathrin-coated pits and drives their invagination
eLife · 2025-08-15
Abstract Clathrin-mediated endocytosis (CME) is essential for maintaining cellular homeostasis. Previous studies have reported more than 50 CME accessory proteins; however, the mechanism driving the invagination of clathrin-coated pits (CCPs) remains elusive. We show by quantitative live cell imaging that siRNA-mediated knockdown of CCDC32, a poorly characterized endocytic accessory protein, leads to the accumulation of unstable flat clathrin assemblies. CCDC32 interacts with the α-appendage domain (AD) of AP2 in vitro and with full length AP2 complexes in cells. Deletion of aa78-98 in CCDC32, corresponding to a predicted α-helix, abrogates AP2 binding and CCDC32’s early function in CME. Furthermore, clinically observed nonsense mutations in CCDC32, which result in C-terminal truncations that lack aa78-98, are linked to the development of cardio-facio-neuro-developmental syndrome (CFNDS). Overall, our data demonstrate the function of a novel endocytic accessory protein, CCDC32, in regulating CCP stabilization and invagination, critical early stages of CME.
bioRxiv (Cold Spring Harbor Laboratory) · 2025-03-30
SUMMARY Cell migration is crucial for development and tissue homeostasis, while its dysregulation leads to severe pathologies. Cell migration is driven by the extension of actin-based lamellipodia protrusions, powered by actin polymerization, which is tightly regulated by signaling pathways, including Rho GTPases and Ca 2+ signaling. While the importance of Ca 2+ signaling in lamellipodia protrusions has been established, the molecular mechanisms linking Ca 2+ to lamellipodia assembly are unknown. Here, we identify a novel Ca 2+ signaling axis involving the mechano-gated channel TRPV4, which regulates lamellipodia protrusions in various cell types. Using Ca 2+ and FRET imaging, we demonstrate that TRPV4-mediated Ca 2+ influx upregulates RhoA activity within lamellipodia, which then facilitates formin-mediated actin assembly. Mechanistically, we identify CaMKII and TEM4 as key mediators relaying the TRPV4-mediated Ca 2+ signal to RhoA. These data define a molecular pathway by which Ca 2+ influx regulates small GTPase activity within a specific cellular domain – lamellipodia - and demonstrate the critical role in organizing the actin machinery and promoting cell migration in diverse biological contexts.
NIH · $307k · 2009
NIH · $1.6M · 2018
Multifaceted roles of nonmuscle myosin II in cell adhesion and migration
NIH · $2.7M · 2013–2022
NIH · $2.7M · 2013
NIH · $27.0M · 2020
Changsong Yang
Gary G. Borisy
Marine Biological Laboratory
Alexander B. Verkhovsky
École Polytechnique Fédérale de Lausanne
Farida Korobova
Northwestern University
Maria S. Shutova
University of Geneva
Ph.D., Cell Biology
University of California, San Francisco
M.S., Cell Biology
University of California, San Francisco
B.S., Cell Biology
University of California, San Francisco
PhdFit ranks faculty by your research interests, methods, and publications — grounded in their actual work, not templates.
Nadia Efimova
Vanderbilt University
Giorgio Scita
FIRC Institute of Molecular Oncology
Alexander D. Bershadsky
National University of Singapore