Solution NMR Backbone Assignment of the C-Terminal Region of Human Dynein Light Intermediate Chain 2 (LIC2-C) Unveils Structural Resemblance with Its Homologue LIC1-C

Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC hom...

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Veröffentlicht in:Magnetochemistry Jg. 9; H. 7; S. 166
Hauptverfasser: Henen, Morkos A., Paukovich, Natasia, Prekeris, Rytis, Vögeli, Beat
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Switzerland MDPI AG 01.07.2023
Schlagworte:
Adapters
Analysis
Cell division
Chemical equilibrium
Dynein
Experiments
Helices
Homology
human dynein
Identification and classification
LIC2
light intermediate chain
NMR
Nuclear magnetic resonance
Phosphorylation
Properties
Protein expression
Proteins
Software
Spectrum analysis
SSP
Structure
Vertebrates
United States
SSP
human dynein
light intermediate chain
LIC2
ISSN:2312-7481, 2312-7481
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Zusammenfassung:Dynein, a homodimeric protein complex, plays a pivotal role in retrograde transportation along microtubules within cells. It consists of various subunits, among which the light intermediate chain (LIC) performs diverse functions, including cargo adaptor binding. In contrast to the vertebrate LIC homolog LIC1, LIC2 has received relatively limited characterization thus far, despite partially orthogonal functional roles. In this study, we present a near-to-complete backbone NMR chemical shift assignment of the C-terminal region of the light intermediate chain 2 of human dynein 1 (LIC2-C). We perform a comparative analysis of the secondary structure propensity of LIC2-C with the one previously reported for LIC1-C and show that the two transient helices in LIC1 that interact with motor adaptors are also present in LIC2.
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Author Contributions: M.A.H., R.P. and B.V. conceptualized the project. M.A.H. and B.V. wrote the manuscript. M.A.H. and N.P. carried out experiments. M.A.H. analyzed data. B.V. and M.A.H. supervised the project and acquired funding. All authors have read and agreed to the published version of the manuscript.
ISSN:2312-7481
2312-7481
DOI:10.3390/magnetochemistry9070166