Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes.
Plasmodium falciparum (Pf) has a family of 11 Rab GTPases to regulate its vesicular transport. However, PfRab5B is unique in lacking a C-terminal geranyl-geranylation motif, while having N-terminal palmitoylation and myristoylation motifs. We show that the N-terminal glycine is required for PfRab5B...
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oai:doaj.org-article:eacfb069e5184d169608c62da8a921452021-11-18T08:34:13ZPlasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes.1932-620310.1371/journal.pone.0087695https://doaj.org/article/eacfb069e5184d169608c62da8a921452014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24498355/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203Plasmodium falciparum (Pf) has a family of 11 Rab GTPases to regulate its vesicular transport. However, PfRab5B is unique in lacking a C-terminal geranyl-geranylation motif, while having N-terminal palmitoylation and myristoylation motifs. We show that the N-terminal glycine is required for PfRab5B myristoylation in vitro and when an N-terminal PfRab5B fragment possessing both acylation motifs is fused to GFP and expressed in transgenic P. falciparum parasites, the chimeric PfRab5B protein localizes to the plasma membrane. Upon substitution of the modified glycine by alanine the staining becomes diffuse and GFP is found in soluble subcellular fractions. Immuno-electron microscopy shows endogenous PfRab5B decorating the parasite's plasma and food vacuole membranes. Using reverse genetics rab5b couldn't be deleted from the haploid genome of asexual blood stage P. berghei parasites. The failure of PbRab5A or PbRab5C to complement for loss of PbRab5B function indicates non-overlapping roles for the three Plasmodium Rab5s, with PfRab5B involved in trafficking MSP1 to the food vacuole membrane and CK1 to the plasma membrane. We discuss similarities between Plasmodium Rab5B and Arabidopsis thaliana ARA6, a similarly unusual Rab5-like GTPase of plants.Carinne Ndjembo EzougouFathia Ben-RachedDavid K MossJing-Wen LinSally BlackEllen KnuepferJudith L GreenShahid M KhanAmitabha MukhopadhyayChris J JanseIsabelle CoppensHélène YeraAnthony A HolderGordon LangsleyPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 2, p e87695 (2014) |
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Medicine R Science Q |
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Medicine R Science Q Carinne Ndjembo Ezougou Fathia Ben-Rached David K Moss Jing-Wen Lin Sally Black Ellen Knuepfer Judith L Green Shahid M Khan Amitabha Mukhopadhyay Chris J Janse Isabelle Coppens Hélène Yera Anthony A Holder Gordon Langsley Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes. |
| description |
Plasmodium falciparum (Pf) has a family of 11 Rab GTPases to regulate its vesicular transport. However, PfRab5B is unique in lacking a C-terminal geranyl-geranylation motif, while having N-terminal palmitoylation and myristoylation motifs. We show that the N-terminal glycine is required for PfRab5B myristoylation in vitro and when an N-terminal PfRab5B fragment possessing both acylation motifs is fused to GFP and expressed in transgenic P. falciparum parasites, the chimeric PfRab5B protein localizes to the plasma membrane. Upon substitution of the modified glycine by alanine the staining becomes diffuse and GFP is found in soluble subcellular fractions. Immuno-electron microscopy shows endogenous PfRab5B decorating the parasite's plasma and food vacuole membranes. Using reverse genetics rab5b couldn't be deleted from the haploid genome of asexual blood stage P. berghei parasites. The failure of PbRab5A or PbRab5C to complement for loss of PbRab5B function indicates non-overlapping roles for the three Plasmodium Rab5s, with PfRab5B involved in trafficking MSP1 to the food vacuole membrane and CK1 to the plasma membrane. We discuss similarities between Plasmodium Rab5B and Arabidopsis thaliana ARA6, a similarly unusual Rab5-like GTPase of plants. |
| format |
article |
| author |
Carinne Ndjembo Ezougou Fathia Ben-Rached David K Moss Jing-Wen Lin Sally Black Ellen Knuepfer Judith L Green Shahid M Khan Amitabha Mukhopadhyay Chris J Janse Isabelle Coppens Hélène Yera Anthony A Holder Gordon Langsley |
| author_facet |
Carinne Ndjembo Ezougou Fathia Ben-Rached David K Moss Jing-Wen Lin Sally Black Ellen Knuepfer Judith L Green Shahid M Khan Amitabha Mukhopadhyay Chris J Janse Isabelle Coppens Hélène Yera Anthony A Holder Gordon Langsley |
| author_sort |
Carinne Ndjembo Ezougou |
| title |
Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes. |
| title_short |
Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes. |
| title_full |
Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes. |
| title_fullStr |
Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes. |
| title_full_unstemmed |
Plasmodium falciparum Rab5B is an N-terminally myristoylated Rab GTPase that is targeted to the parasite's plasma and food vacuole membranes. |
| title_sort |
plasmodium falciparum rab5b is an n-terminally myristoylated rab gtpase that is targeted to the parasite's plasma and food vacuole membranes. |
| publisher |
Public Library of Science (PLoS) |
| publishDate |
2014 |
| url |
https://doaj.org/article/eacfb069e5184d169608c62da8a92145 |
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