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Status: Bibliographieeintrag

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Verfasst von:Dimitrova-Paternoga, Lyudmila Nikolova [VerfasserIn]   i
 Jagtap, Pravin Kumar Ankush [VerfasserIn]   i
 Cyrklaff, Anna [VerfasserIn]   i
 Vaishali [VerfasserIn]   i
 Lapouge, Karine [VerfasserIn]   i
 Sehr, Peter [VerfasserIn]   i
 Perez, Kathryn [VerfasserIn]   i
 Heber, Simone [VerfasserIn]   i
 Löw, Christian [VerfasserIn]   i
 Hennig, Janosch [VerfasserIn]   i
 Ephrussi, Anne [VerfasserIn]   i
Titel:Molecular basis of mRNA transport by a kinesin-1-atypical tropomyosin complex
Verf.angabe:Lyudmila Dimitrova-Paternoga, Pravin Kumar Ankush Jagtap, Anna Cyrklaff, Vaishali, Karine Lapouge, Peter Sehr, Kathryn Perez, Simone Heber, Christian Löw, Janosch Hennig, and Anne Ephrussi
Jahr:2021
Umfang:16 S.
Fussnoten:Gesehen am 26.09.2021
Titel Quelle:Enthalten in: Genes & development
Ort Quelle:Stanford, Calif. : HighWire Press, 1987
Jahr Quelle:2021
Band/Heft Quelle:35(2021), 13/14, Seite 976-991
ISSN Quelle:1549-5477
Abstract:Kinesin-1 carries cargos including proteins, RNAs, vesicles, and pathogens over long distances within cells. The mechanochemical cycle of kinesins is well described, but how they establish cargo specificity is not fully understood. Transport of oskar mRNA to the posterior pole of the Drosophila oocyte is mediated by Drosophila kinesin-1, also called kinesin heavy chain (Khc), and a putative cargo adaptor, the atypical tropomyosin, aTm1. How the proteins cooperate in mRNA transport is unknown. Here, we present the high-resolution crystal structure of a Khc-aTm1 complex. The proteins form a tripartite coiled coil comprising two in-register Khc chains and one aTm1 chain, in antiparallel orientation. We show that aTm1 binds to an evolutionarily conserved cargo binding site on Khc, and mutational analysis confirms the importance of this interaction for mRNA transport in vivo. Furthermore, we demonstrate that Khc binds RNA directly and that it does so via its alternative cargo binding domain, which forms a positively charged joint surface with aTm1, as well as through its adjacent auxiliary microtubule binding domain. Finally, we show that aTm1 plays a stabilizing role in the interaction of Khc with RNA, which distinguishes aTm1 from classical motor adaptors.
DOI:doi:10.1101/gad.348443.121
URL:Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.

Volltext ; Verlag: https://doi.org/10.1101/gad.348443.121
 Volltext: http://genesdev.cshlp.org/content/35/13-14/976
 DOI: https://doi.org/10.1101/gad.348443.121
Datenträger:Online-Ressource
Sprache:eng
Sach-SW:kinesin
 kinesin adaptor
 kinesin-atypical tropomyosin complex
 mRNA transport
 oskar mRNA
K10plus-PPN:1771804769
Verknüpfungen:→ Zeitschrift

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