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Overview

Our Mission

My lab investigates pathogenesis of age-dependent neurodegenerative diseases, like Alzheimer's disease and Parkinson's disease, at the cellular-molecular level. To study these diseases, we combine biochemistry, cell biology, mouse genetic models and mouse behavior.

Short-term Goals

Neurodegenerative diseases are associated with varied genetic and environmental factors, yet age remains a universal risk factor. Age-associated failure of protein homeostasis, or “proteostasis”, causes disease-linked proteins to misfold into non-physiological oligomers and aggregates, producing a myriad of cellular dysfunctions. Long lifetime of a neuron enhances the need for proteostatic mechanisms, such as molecular chaperones that stabilize native protein folds and degradation pathways that eliminate misfolded proteins. My lab is interested in the mechanisms that mediate proteostasis in neurons and how their failure over time leads to neurodegeneration.

We are investigating this topic by:
a) Studying how proteostasis of Tau protein is regulated by two co-chaperones of Hsc70: CHIP (C-terminus of Hsc/Hsp70 interacting protein) and CSP-α (cysteine string protein-α).
b) Investigating how neurodegeneration is caused by recently found human mutations in CSP-α which cause neuronal ceroid lipofuscinosis, an adult-onset neurodegenerative disorder.
c) Comparing lysosomes from brains of normal mice and from neurodegenerative mouse models to identify changes that accompany the decline of neuronal proteostasis.

Long-term Goals

Our research will uncover proteostatic mechanisms in neurons which allow them to live and function for a lifetime, and how these mechanisms fail in aging neurons. Understanding neuronal proteostasis in health and disease may lead to treatment strategies for multiple neurodegenerative disorders, like Parkinson’s disease and Alzheimer’s disease, which share age-dependent proteostatic defects.

Highlights

  1. 1
    Nature communications · 2022
    PMID: 35995799PMCID: PMC9395532DOISenior author91 citations
  2. 2
    Nature structural & molecular biology · 2020
    PMID: 32042150PMCID: PMC7021000DOISenior author17 citations

Publications

37 publications

Active

5 grants
  • MPI
    Changes in synaptic vesicle-binding of alpha-synuclein as an early biomarker for synucleinopathies
    National Institute of Neurological Disorders and Stroke · 2024–2029
    R01NS136423-01A1
  • MPI
    Tau proteostasis by chaperone-complexes in tauopathies including Alzheimer's disease
    National Institute on Aging · 2024–2029
    R01AG083949-03
  • Co-I
    Small molecule inhibitors of CAPON-induced tau aggregation
    National Institute on Aging · 2024–2027
    RF1AG084635-01A1
  • KP
    Mechanism and rescue of lysosomal defects in Adult-onset Neuronal Ceroid Lipofuscinosis
    National Institute of Neurological Disorders and Stroke · 2025–2027Fellowship
    F31NS143430-01A1
  • MPI
    The impact of beta- and gamma-synucleins on alpha-synuclein's synaptic function
    National Institute of Neurological Disorders and Stroke · 2022–2027
    R01NS126342-02
Completed grants (4)
  • PI
    Cellular Mechanism of Adult Onset Neuronal Ceroid Lipofuscinosis (ANCL) Caused by Mutations in Cysteine String Protein-Alpha (CSPalpha)
    National Institute of Neurological Disorders and Stroke · 2017–2025
    R01NS095988-05
  • PI
    DnaJ Co-Chaperones Which Modify Tau Aggregation and Neurodegeneration
    National Institute on Aging · 2016–2024
    R01AG052505-05
  • KP
    Biophysical Characterization of Covalently Modified Protein Tau: Oligomers, Aggregation, and Tubulin Interactions
    National Institute on Aging · 2020–2022Fellowship
    F31AG069416-01
  • KP
    Disease Causing Mutations in Cysteine String Protein-Alpha Disrupt SNARE-Dependent Lysosomal Exocytosis
    National Institute of Neurological Disorders and Stroke · 2017–2020Fellowship
    F31NS098623-02

Available technologies

News mentions