دورية أكاديمية

Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility

التفاصيل البيبلوغرافية
العنوان: Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light chain required for maximum motility
المؤلفون: Green, Judith L., Wall, Richard J., Vahokoski, Juha, Yusuf, Noor A., Mohd Ridzuan, Mohd A., Stanway, Rebecca R., Stock, Jessica, Knuepfer, Ellen, Brady, Declan, Martin, Stephen R., Howell, Steven A., Pires, Isa P., Moon, Robert W., Molloy, Justin E., Kursula, Inari, Tewari, Rita, Holder, Anthony A.
المصدر: Green , J L , Wall , R J , Vahokoski , J , Yusuf , N A , Mohd Ridzuan , M A , Stanway , R R , Stock , J , Knuepfer , E , Brady , D , Martin , S R , Howell , S A , Pires , I P , Moon , R W , Molloy , J E , Kursula , I , Tewari , R & Holder , A A 2017 , ' Compositional and expression analyses of the glideosome during the Plasmodium life cycle reveal an additional myosin light ....
سنة النشر: 2017
المجموعة: Discovery - University of Dundee Online Publications
مصطلحات موضوعية: cell motility, invastion, malaria, myosin, plasmodium, glideosome, myosin light chain, /dk/atira/pure/subjectarea/asjc/1300/1303, name=Biochemistry, /dk/atira/pure/subjectarea/asjc/1300/1312, name=Molecular Biology, /dk/atira/pure/subjectarea/asjc/1300/1307, name=Cell Biology
الوصف: Myosin A (MyoA) is a Class XIV myosin implicated in gliding motility and host cell and tissue invasion by malaria parasites. MyoA is part of a membrane-associated protein complex called the glideosome, which is essential for parasite motility and includes the MyoA light chain myosin tail domain–interacting protein (MTIP) and several glideosome-associated proteins (GAPs). However, most studies of MyoA have focused on single stages of the parasite life cycle. We examined MyoA expression throughout the Plasmodium berghei life cycle in both mammalian and insect hosts. In extracellular ookinetes, sporozoites, and merozoites, MyoA was located at the parasite periphery. In the sexual stages, zygote formation and initial ookinete differentiation precede MyoA synthesis and deposition, which occurred only in the developing protuberance. In developing intracellular asexual blood stages, MyoA was synthesized in mature schizonts and was located at the periphery of segmenting merozoites, where it remained throughout maturation, merozoite egress, and host cell invasion. Besides the known GAPs in the malaria parasite, the complex included GAP40, an additional myosin light chain designated essential light chain (ELC), and several other candidate components. This ELC bound the MyoA neck region adjacent to the MTIP-binding site, and both myosin light chains co-located to the glideosome. Co-expression of MyoA with its two light chains revealed that the presence of both light chains enhances MyoA-dependent actin motility. In conclusion, we have established a system to study the interplay and function of the three glideosome components, enabling the assessment of inhibitors that target this motor complex to block host cell invasion.
نوع الوثيقة: article in journal/newspaper
وصف الملف: application/pdf
اللغة: English
العلاقة: https://discovery.dundee.ac.uk/en/publications/d1dec8db-ea85-4051-8bc4-a6a87aab1a03Test
DOI: 10.1074/jbc.M117.802769
الإتاحة: https://doi.org/10.1074/jbc.M117.802769Test
https://discovery.dundee.ac.uk/en/publications/d1dec8db-ea85-4051-8bc4-a6a87aab1a03Test
https://discovery.dundee.ac.uk/ws/files/19127686/J._Biol._Chem._2017_Green_17857_75.pdfTest
حقوق: info:eu-repo/semantics/openAccess
رقم الانضمام: edsbas.71D570EE
قاعدة البيانات: BASE