Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism. Export

@article{citeulike:2869357, abstract = {Plasmodium falciparum, the causative agent of malaria, relies on a complex protein-secretion system for protein targeting into numerous subcellular destinations. Recently, a homologue of the Golgi re-assembly stacking protein (GRASP) was identified and used to characterise the Golgi organisation in this parasite. Here, we report on the presence of a splice variant that leads to the expression of a GRASP isoform. Although the first GRASP protein (GRASP1) relies on a well-conserved myristoylation motif, the variant (GRASP2) displays a different N-terminus, similar to GRASPs found in fungi. Phylogenetic analyses between GRASP proteins of numerous taxa point to an independent evolution of the unusual N-terminus that could reflect unique requirements for Golgi-dependent protein sorting and organelle biogenesis in P. falciparum. Golgi association of GRASP2 depends on the hydrophobic N-terminus that resembles a signal anchor, leading to a unique mode of Golgi targeting and membrane attachment.}, author = {Struck, Nicole S S. and Herrmann, Susann and Langer, Christine and Krueger, Andreas and Foth, Bernardo J J. and Engelberg, Klemens and Cabrera, Ana L L. and Haase, Silvia and Treeck, Moritz and Marti, Matthias and Cowman, Alan F F. and Spielmann, Tobias and Gilberger, Tim W W.}, citeulike-article-id = {2869357}, citeulike-linkout-0 = {http://dx.doi.org/10.1242/jcs.021154}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/18522993}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=18522993}, day = {3}, doi = {10.1242/jcs.021154}, issn = {0021-9533}, journal = {Journal of cell science}, keywords = {golgi, grasp}, month = {June}, posted-at = {2008-06-06 13:55:04}, priority = {2}, title = {Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism.}, url = {http://dx.doi.org/10.1242/jcs.021154}, year = {2008} }

TY - JOUR ID - citeulike:2869357 L3 - citeulike-article-id:2869357 N2 - Plasmodium falciparum, the causative agent of malaria, relies on a complex protein-secretion system for protein targeting into numerous subcellular destinations. Recently, a homologue of the Golgi re-assembly stacking protein (GRASP) was identified and used to characterise the Golgi organisation in this parasite. Here, we report on the presence of a splice variant that leads to the expression of a GRASP isoform. Although the first GRASP protein (GRASP1) relies on a well-conserved myristoylation motif, the variant (GRASP2) displays a different N-terminus, similar to GRASPs found in fungi. Phylogenetic analyses between GRASP proteins of numerous taxa point to an independent evolution of the unusual N-terminus that could reflect unique requirements for Golgi-dependent protein sorting and organelle biogenesis in P. falciparum. Golgi association of GRASP2 depends on the hydrophobic N-terminus that resembles a signal anchor, leading to a unique mode of Golgi targeting and membrane attachment. JF - Journal of cell science SN - 0021-9533 TI - Plasmodium falciparum possesses two GRASP proteins that are differentially targeted to the Golgi complex via a higher- and lower-eukaryote-like mechanism. KW - golgi KW - grasp AU - Struck, Nicole S AU - Herrmann, Susann AU - Langer, Christine AU - Krueger, Andreas AU - Foth, Bernardo J AU - Engelberg, Klemens AU - Cabrera, Ana L AU - Haase, Silvia AU - Treeck, Moritz AU - Marti, Matthias AU - Cowman, Alan F AU - Spielmann, Tobias AU - Gilberger, Tim W PY - 2008/06/03/ UR - http://dx.doi.org/10.1242/jcs.021154 ER -