
WU Min
Collaborator, Mechanobiology Institute, National University of Singapore
dbswum@nus.edu.sg
+65 6601 2310
CBIS Blk S1A, Level 2 Lee Wee Kheng Bldg
National University of Singapore
14 Science Drive 4
Singapore 117557
Laboratory website
Wu Lab Deconstructing the Endocytic Machinery
Research Program
The Cell-Matrix and Cell-Cell Mechanotransduction Group
Affiliations
Department of Biological Sciences, National University of Singapore
CHEAM Mei Shan
PhD Student, Class of August 2025, Toyama Group
Thanks to Christiani Amorim at UC Louvain, for the kind invitation
Looking forward to new collaborations in the future!
Congratulations to Wee Juin Shin for being selected to present his work at the Amgen Scholars Asia Symposium!
Our Amgen scholar, Wee Juin Shin, has been selected to present his work on ‘the Influence of substrate curvature on theca cell nematic flow’, at the Amgen Scholar Asia Symposium in Kyoto!
Geetika Chouhan
Research Fellow, Dye Group
Seeking Research Assistant for project with MBI Fellow Dr. Tee Yee Han at the Mechanobiology Institute, NUS
The Mechanobiology Institute, NUS seeks to recruit a Research Assistant to work with MBI Fellow Dr. Tee Yee Han.
Seeking Research Fellow in the group of Prof. Alexander Bershadsky at the Mechanobiology Institute, NUS
The Mechanobiology Institute, NUS seeks to recruit a Research Fellow in the group of Prof. Alexander Bershadsky at the MBI, NUS.
Wu Min
Collaborator
Research Areas
Endocytosis, Membrane traffic, Curvature, Actin cytoskeleton, Mechanotransduction
Research Interests
Dr Wu is interested in elucidating the principles underlying the organization and dynamics of the subcellular membrane compartments. Specifically her lab investigates how biological membranes are shaped through collective protein-lipid interactions and how geometry of the membrane compartment is coupled to cellular functions. The Wu Lab uses a combination of cell biological, biophysical and biochemical approaches to address these questions.
Biography
Dr Wu Min graduated from Peking University in China and received her bachelor degree in Chemistry. She did her graduate studies at Cornell University with Dr Barbara Baird, where she initiated the use of patterned lipid bilayers as antigen-presenting platforms and studied immune cell activation and signal transduction. During her post-doctoral research in the laboratory of Dr Pietro De Camilli at Yale School of Medicine, she focused on the molecular mechanisms of endocytosis. In 2011, she was awarded the NRF fellowship, joining CBIS/MBI in the fall.
Education
PhD Cornell University
Recent Publications
- Xiong D, Tong C, Fung SYS, McClellan S, Yang Y, Yong J, and Wu M. STIM1 and endoplasmic reticulum-plasma membrane contact sites oscillate independently of calcium-induced calcium release. Open Biol 2026; 16(3). [PMID: 41844235]
- Chua XL, Tong CS, Su M, Xǔ XJ, Xiao S, Wu X, and Wu M. Competition and synergy of Arp2/3 and formins in nucleating actin waves. Cell Rep 2024; 43(7):114423. [PMID: 38968072]
- Tong CS, Su M, Sun H, Chua XL, Xiong D, Guo S, Raj R, Ong NWP, Lee AG, Miao Y, and Wu M. Collective dynamics of actin and microtubule and its crosstalk mediated by FHDC1. Front Cell Dev Biol 2024; 11:1261117. [PMID: 38567385]
- Le Chua X, Tong CS, Xǔ XJ, Su M, Xiao S, Wu X, and Wu M. Competition and Synergy of Arp2/3 and Formins in Nucleating Actin Waves. bioRxiv 2023;. [PMID: 37745345]
- Su M, Zhuang Y, Miao X, Zeng Y, Gao W, Zhao W, and Wu M. Comparative Study of Curvature Sensing Mediated by F-BAR and an Intrinsically Disordered Region of FBP17. iScience 2020; 23(11):101712. [PMID: 33205024]
- Chen Y, Yong J, Martínez-Sánchez A, Yang Y, Wu Y, De Camilli P, Fernández-Busnadiego R, and Wu M. Dynamic instability of clathrin assembly provides proofreading control for endocytosis. J. Cell Biol. 2019;. [PMID: 31451612]
- . https://www.ncbi.nlm.nih.gov/pubmed/31390543
- Yong J, Chen Y, and Wu M. Real-Time Monitoring of Clathrin Assembly Kinetics in a Reconstituted System. Methods Mol. Biol. 2018; 1847:177-187. [PMID: 30129017]
- Yang Y, and Wu M. Rhythmicity and waves in the cortex of single cells. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 2018; 373(1747). [PMID: 29632268]
- McPherson PS, and Wu M. Light, space, and time in cancer signaling. Mol. Biol. Cell 2018; 29(6):688. [PMID: 29535172]
Lab Members
What is the role of cortactin in actin polymerization?
What is the role of cortactin in actin polymerization? Cortactin is a class II nucleation promoting factor (NPF) that binds to actin filaments and influences their stability. Cortactin specifically stabilizes Arp2/3-mediated branch points along [...]
Actin Crosslinking
Actin Crosslinking Crosslinking of actin filaments is a critical step in cell motility and is a fundamental process in filopodia protrusion and lamellipodia formation. Smaller cross-linking proteins that are more globular (e.g. fascin) [...]
What is the role of formin in actin polymerization?
What is the role of formin in actin polymerization? Formins promote the elongation of pre-existing filaments by removing barbed end capping proteins and forming a sleeve around the actin subunits. Formins are also capable [...]
What is the steady state phase of actin polymerization?
What is the steady state phase of actin polymerization? In the steady state phase, the filament dynamics enter a state of equilibrium where monomer disassembly from the (-) end and polymerization at the (+) [...]
What factors influence actin filament length and treadmilling?
What factors influence actin filament length and treadmilling? Several factors influence actin filament length and treadmilling. ATP binding on G-actin and free ATP-G-actin concentration ATP-binding on actin subunits modulates the dynamics of filament assembly, [...]
What factors regulate actin filament polymerization?
What factors regulate actin filament polymerization? Nucleation Promoting Factors (NPFs) (e.g. WASP, Scar/WAVE) modulate actin filament nucleation by bringing together actin monomers and pre-existing actin filaments, for example, during filopodial initiation where they recruit [...]
What are microtubules?
What are microtubules? Microtubules are hollow cylinders [1] that are approximately 25nm in diameter [2] and vary in length from 200 nm to 25 μm. They are formed by the lateral association of between [...]
How are intermediate filaments assembled?
How are intermediate filaments assembled? The soluble subunit for creating intermediate filaments is a tetramer. The tetramer is created from monomers in a stepwise fashion (as reviewed in [1]). First, two monomers associate via [...]
What are intermediate filaments?
What are intermediate filaments? Intermediate filaments are a primary component of the cytoskeleton, although they are not found in all eukaryotes, and are absent in fungi and plants [1]. These filaments, which extend throughout [...]
I-BAR and Other Proteins/Factors
I-BAR and Other Proteins/Factors Proteins containing I-BAR (inverted Bin/amphiphysin/Rvs i.e. IRSp53 Missing-in-metastasis homology Domain or IMD) cooperate with various components of actin filament assembly, to promote filopodia protrusion, via several mechanisms including the stimulation [...]
Fimbrin
Fimbrin Fimbrin (aka plastin homologue, accumentin) is an actin binding protein that was originally identified in microvilli [1][2]. This schematic diagram illustrates the molecular organization of fimbrin as depicted in this resource, and [...]
Filamin
Filamin The filamin family of proteins bind to both actin and a number of signaling molecules including Rho GTPases. Evidence for this was shown with the loss of Filamin-A in M2 Melanoma cells, which [...]

