Kinetoplastid-specific X2-family kinesins interact with a kinesin-like pleckstrin homology domain protein that localizes to the trypanosomal microtubule quartet

Benz, Corinna; Müller, N.; Kaltenbrunner, Sabine; Váchová, Hana; Vancová, Marie; Lukeš, Julius; Varga, Vladimír; Hashimi, Hassan

doi:https://dx.doi.org/10.1111/mmi.14958

Number of the records: 1

Kinetoplastid-specific X2-family kinesins interact with a kinesin-like pleckstrin homology domain protein that localizes to the trypanosomal microtubule quartet

1.

SYSNO ASEP	0561336
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Kinetoplastid-specific X2-family kinesins interact with a kinesin-like pleckstrin homology domain protein that localizes to the trypanosomal microtubule quartet
Author(s)	Benz, Corinna (BC-A)_{RID, ORCID} Müller, N. (CZ) Kaltenbrunner, Sabine (BC-A)_ORCID Váchová, Hana (UMG-J) Vancová, Marie (BC-A)_{RID, ORCID} Lukeš, Julius (BC-A)_{RID, ORCID} Varga, Vladimír (UMG-J)_ORCID Hashimi, Hassan (BC-A)_{RID, ORCID}
Number of authors	8
Source Title	Molecular Microbiology - ISSN 0950-382X Roč. 118, č. 3 (2022), s. 155-174
Number of pages	20 s.
Publication form	Print - P
Language	eng - English
Country	GB - United Kingdom
Keywords	cytoskeleton ; kinesin ; microtubule quartet ; microtubules ; morphogenesis ; Trypanosoma
Subject RIV	EE - Microbiology, Virology
OECD category	Microbiology
Subject RIV - cooperation	Institute of Molecular Genetics - Genetics ; Molecular Biology
R&D Projects	EF16_019/0000759 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	LM2018129 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	LL1601 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	GA20-23513S GA ČR - Czech Science Foundation (CSF)
	GA21-09283S GA ČR - Czech Science Foundation (CSF)
Method of publishing	Limited access
Institutional support	BC-A - RVO:60077344 ; UMG-J - RVO:68378050
UT WOS	000824783600001
EID SCOPUS	85134067856
DOI	10.1111/mmi.14958
Annotation	Kinesins are motor proteins found in all eukaryotic lineages that move along microtubules to mediate cellular processes such as mitosis and intracellular transport. In trypanosomatids, the kinesin superfamily has undergone a prominent expansion, resulting in one of the most diverse kinesin repertoires that includes the two kinetoplastid-restricted families X1 and X2. Here, we characterize in Trypanosoma brucei TbKifX2A, an orphaned X2 kinesin. TbKifX2A tightly interacts with TbPH1, a kinesin-like protein with a likely inactive motor domain, a rarely reported occurrence. Both TbKifX2A and TbPH1 localize to the microtubule quartet (MtQ), a characteristic but poorly understood cytoskeletal structure that wraps around the flagellar pocket as it extends to the cell body anterior. The proximal proteome of TbPH1 revealed two other interacting proteins, the flagellar pocket protein FP45 and intriguingly another X2 kinesin, TbKifX2C. Simultaneous ablation of TbKifX2A/TbPH1 results in the depletion of FP45 and TbKifX2C and also an expansion of the flagellar pocket, among other morphological defects. TbKifX2A is the first motor protein to be localized to the MtQ. The observation that TbKifX2C also associates with the MtQ suggests that the X2 kinesin family may have co-evolved with the MtQ, both kinetoplastid-specific traits.
Workplace	Biology Centre (since 2006)
Contact	Dana Hypšová, eje@eje.cz, Tel.: 387 775 214
Year of Publishing	2023
Electronic address	https://onlinelibrary.wiley.com/doi/10.1111/mmi.14958

Number of the records: 1