المؤلفون: Mana Giulia, Clapero Fabiana, Panieri Emiliano, Panero Valentina, Böttcher Ralph T, Tseng Hui Yuan, Saltarin Federico, Astanina Elena, Wolanska Katarzyna I, Morgan Mark R, Humphries Martin J, Serini Guido, Valdembri Donatella, SANTORO, MASSIMO

المساهمون: Mana, Giulia, Clapero, Fabiana, Panieri, Emiliano, Panero, Valentina, Böttcher Ralph, T, Tseng Hui, Yuan, Saltarin, Federico, Astanina, Elena, Wolanska Katarzyna, I, Morgan Mark, R, Humphries Martin, J, Santoro, Massimo, Serini, Guido, Valdembri, Donatella

مصطلحات موضوعية: Integrin, Angiogenesi, Endothelial Cell, Endocytosi, Trans-Golgi network, Fibronectin, Embryonic development, Zebrafish

الوصف: Basolateral polymerization of cellular fibronectin (FN) into a meshwork drives endothelial cell (EC) polarity and vascular remodelling. However, mechanisms coordinating α5β1 integrin-mediated extracellular FN endocytosis and exocytosis of newly synthesized FN remain elusive. Here we show that, on Rab21-elicited internalization, FN-bound/active α5β1 is recycled to the EC surface. We identify a pathway, comprising the regulators of post-Golgi carrier formation PI4KB and AP-1A, the small GTPase Rab11B, the surface tyrosine phosphatase receptor PTPRF and its adaptor PPFIA1, which we propose acts as a funnel combining FN secretion and recycling of active α5β1 integrin from the trans-Golgi network (TGN) to the EC surface, thus allowing FN fibrillogenesis. In this framework, PPFIA1 interacts with active α5β1 integrin and localizes close to EC adhesions where post-Golgi carriers are targeted. We show that PPFIA1 is required for FN polymerization-dependent vascular morphogenesis, both in vitro and in the developing zebrafish embryo.

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/27876801; info:eu-repo/semantics/altIdentifier/wos/WOS:000388323000001; volume:7; firstpage:13546; lastpage:13565; numberofpages:20; journal:NATURE COMMUNICATIONS; http://hdl.handle.net/11577/3242244Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-84997108022; http://www.nature.com/articles/ncomms13546Test

الإتاحة: https://doi.org/10.1038/ncomms13546Test
http://hdl.handle.net/11577/3242244Test
http://www.nature.com/articles/ncomms13546Test

المؤلفون: Di Cristina M., Spaccapelo R., Soldati D., Bistoni F., Crisanti A.

المساهمون: Di Cristina, M., Spaccapelo, R., Soldati, D., Bistoni, F., Crisanti, A.

مصطلحات موضوعية: SPOROZOITE SURFACE PROTEIN-2, TRANS-GOLGI NETWORK, CYTOPLASMIC DOMAIN, PLASMODIUM-BERGHEI, MEMBRANE-PROTEINS, ENDOCYTIC PATHWAY, GLIDING MOTILITY, DUFFY RECEPTOR, THROMBOSPONDIN, SEQUENCE

الوصف: The micronemal protein 2 (MIC2) of Toxoplasma gondii shares sequence and structural similarities with a series of adhesive molecules of different apicomplexan parasites. These molecules accumulate, through a yet unknown mechanism, in secretory vesicles (micronemes), which together with tubular and membrane structures form the locomotion and invasion machinery of apicomplexan parasites. Our findings indicated that two conserved motifs placed within the cytoplasmic domain of MIC2 are both necessary and sufficient for targeting proteins to T. gondii micronemes. The first motif is based around the amino acid sequence SYHYY. Database analysis revealed that a similar sequence is present in the cytoplasmic tail of all transmembrane micronemal proteins identified so far in different apicomplexan species. The second signal consists of a stretch of acidic residues, EIEYE. The creation of an artificial tail containing only the two motifs SYHYY and EIEYE in a preserved spacing configuration is sufficient to target the surface protein SAG1 to the micronemes of T. gondii. These findings shed new light on the molecular mechanisms that control the formation of the microneme content and the functional relationship that links these organelles with the endoplasmic reticulum of the parasite.

وصف الملف: STAMPA

العلاقة: info:eu-repo/semantics/altIdentifier/pmid/10982850; info:eu-repo/semantics/altIdentifier/wos/WOS:000089268700030; volume:20; issue:19; firstpage:7332; lastpage:7341; numberofpages:10; journal:MOLECULAR AND CELLULAR BIOLOGY; http://hdl.handle.net/11577/3315084Test; info:eu-repo/semantics/altIdentifier/scopus/2-s2.0-0033830555; http://www.ncbi.nlm.nih.gov/pubmed/10982850Test

الإتاحة: https://doi.org/10.1128/MCB.20.19.7332-7341.2000Test
http://hdl.handle.net/11577/3315084Test
http://www.ncbi.nlm.nih.gov/pubmed/10982850Test