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

Morkos A Henen; Natasia Paukovich; Rytis Prekeris; Beat Vögeli

doi:10.3390/magnetochemistry9070166

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

Magnetochemistry. 2023 Jul;9(7):166. doi: 10.3390/magnetochemistry9070166. Epub 2023 Jun 28.

Authors

Morkos A Henen¹, Natasia Paukovich¹, Rytis Prekeris², Beat Vögeli¹

Affiliations

¹ Department of Biochemistry and Molecular Genetics, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.
² Department of Cell and Developmental Biology, School of Medicine, University of Colorado Anschutz Medical Campus, Aurora, CO 80045, USA.

Abstract

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.

Keywords: LIC2; SSP; human dynein; light intermediate chain.

Abstract

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