Human TBC1 domain-containing kinase is a class I multidomain pseudokinase.

Shiwangi Maurya, Lilly E Cheek, Anthony T Iavarone, Wen Zhu

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Article in Protein expression and purification, 2027. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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Update of
Human TBC1 domain-containing kinase is a class I multidomain pseudokinase.2026

5 · Who and what money

Authors and funding

4 authors.

Shiwangi MauryaDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA.

Lilly E CheekDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA.

Anthony T IavaroneCalifornia Institute for Quantitative Biosciences, University of California, Berkeley, CA, 94720, USA.

Wen ZhuDepartment of Chemistry and Biochemistry, Florida State University, Tallahassee, FL, 32306, USA. Electronic address: wzhu@chem.fsu.edu.

Funding

Linking Conformational Dynamics to Activity Impairment of Disease-associated Human EnzymesR35GM160337 · NIGMS · FLORIDA STATE UNIVERSITY · PI Wen Zhu · 2025 to 2026

$835k

High Definition Ion Mobility SpectrometerS10OD020062 · OD · UNIVERSITY OF CALIFORNIA BERKELEY · PI WILLIAMS, EVAN R · 2015 to 2015

$590k

NIGMS NIH HHS R35 GM160337NIH HHS S10 OD020062

6 · The paper itself

Abstract

TBCK-related encephalopathy (TBCKE) is a neurodevelopmental disorder associated with biallelic mutations in TBCK. Despite the increasing number of reported cases worldwide, the biochemical and biophysical properties of TBCK remain unclear, hindering molecular understanding of its role in disease. Here, we report the successful expression and purification of full-length human TBCK using Spodoptera frugiperda cells. Biochemical and biophysical analyses reveal that the catalytically inactive pseudokinase domain of TBCK lacks nucleotide binding, consistent with the absence of the canonical VAIK, HRD, and DFG motifs required for catalysis. These findings support that TBCK is a class I pseudokinase and provide a foundation for future structural and functional studies to elucidate its biological role.

Indexed as

Protein Serine-Threonine KinasesAnimalsHumansProtein DomainsRecombinant ProteinsSpodopteraProtein Serine-Threonine KinasesRecombinant ProteinsTBCK protein, human

Identifiers

PMID42546825

DOI10.1016/j.pep.2026.106989

PMCPMC13502288

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.