scholarly journals N-terminal palmitoylation is required for Toxoplasma gondii HSP20 inner membrane complex localization

2013 ◽  
Vol 1833 (6) ◽  
pp. 1329-1337 ◽  
Author(s):  
M.G. De Napoli ◽  
N. de Miguel ◽  
M. Lebrun ◽  
S.N.J. Moreno ◽  
S.O. Angel ◽  
...  
2021 ◽  
Vol 100 (2) ◽  
pp. 151149
Author(s):  
Rikako Konishi ◽  
Yuna Kurokawa ◽  
Kanna Tomioku ◽  
Tatsunori Masatani ◽  
Xuenan Xuan ◽  
...  

2004 ◽  
Vol 165 (3) ◽  
pp. 383-393 ◽  
Author(s):  
Elizabeth Gaskins ◽  
Stacey Gilk ◽  
Nicolette DeVore ◽  
Tara Mann ◽  
Gary Ward ◽  
...  

Apicomplexan parasites exhibit a unique form of substrate-dependent motility, gliding motility, which is essential during their invasion of host cells and during their spread between host cells. This process is dependent on actin filaments and myosin that are both located between the plasma membrane and two underlying membranes of the inner membrane complex. We have identified a protein complex in the apicomplexan parasite Toxoplasma gondii that contains the class XIV myosin required for gliding motility, TgMyoA, its associated light chain, TgMLC1, and two novel proteins, TgGAP45 and TgGAP50. We have localized this complex to the inner membrane complex of Toxoplasma, where it is anchored in the membrane by TgGAP50, an integral membrane glycoprotein. Assembly of the protein complex is spatially controlled and occurs in two stages. These results provide the first molecular description of an integral membrane protein as a specific receptor for a myosin motor, and further our understanding of the motile apparatus underlying gliding motility in apicomplexan parasites.


2016 ◽  
Vol 12 (2) ◽  
pp. e1005403 ◽  
Author(s):  
Clare R. Harding ◽  
Saskia Egarter ◽  
Matthew Gow ◽  
Elena Jiménez-Ruiz ◽  
David J. P. Ferguson ◽  
...  

1997 ◽  
Vol 83 (3) ◽  
pp. 252-256 ◽  
Author(s):  
E. J. T. de Melo ◽  
W. de Souza ◽  
E. J. T. de Melo ◽  
W. de Souza

2008 ◽  
Vol 100 (8) ◽  
pp. 479-489 ◽  
Author(s):  
Natalia Miguel ◽  
Maryse Lebrun ◽  
Aoife Heaslip ◽  
Ke Hu ◽  
Con J. Beckers ◽  
...  

PLoS Biology ◽  
2019 ◽  
Vol 17 (10) ◽  
pp. e3000475 ◽  
Author(s):  
Charles Paul Choi ◽  
Andy Seong Moon ◽  
Peter Sungmin Back ◽  
Yasaman Jami‐Alahmadi ◽  
Ajay Amar Vashisht ◽  
...  

2007 ◽  
Vol 18 (8) ◽  
pp. 3039-3046 ◽  
Author(s):  
Terezina M. Johnson ◽  
Zenon Rajfur ◽  
Ken Jacobson ◽  
Con J. Beckers

The substrate-dependent movement of apicomplexan parasites such as Toxoplasma gondii and Plasmodium sp. is driven by the interaction of a type XIV myosin with F-actin. A complex containing the myosin-A heavy chain, a myosin light chain, and the accessory protein GAP45 is attached to the membranes of the inner membrane complex (IMC) through its tight interaction with the integral membrane glycoprotein GAP50. For the interaction of this complex with F-actin to result in net parasite movement, it is necessary that the myosin be immobilized with respect to the parasite and the actin with respect to the substrate the parasite is moving on. We report here that the myosin motor complex of Toxoplasma is firmly immobilized in the plane of the IMC. This does not seem to be accomplished by direct interactions with cytoskeletal elements. Immobilization of the motor complex, however, does seem to require cholesterol. Both the motor complex and the cholesterol are found in detergent-resistant membrane domains that encompass a large fraction of the inner membrane complex surface. The observation that the myosin XIV motor complex of Toxoplasma is immobilized within this cholesterol-rich membrane likely extends to closely related pathogens such as Plasmodium and possibly to other eukaryotes.


2019 ◽  
Vol 22 (1) ◽  
Author(s):  
Klemens Engelberg ◽  
Chun‐Ti Chen ◽  
Tyler Bechtel ◽  
Victoria Sánchez Guzmán ◽  
Allison A. Drozda ◽  
...  

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