<b>Structure, regulation and cellular functions of Rab geranylgeranyl transferase and its cellular partner Rab Escort Protein</b>

Gutkowska, Małgorzata; Świeżewska, Ewa

doi:10.3109/09687688.2012.693211

Cited by 13 publications

(9 citation statements)

References 67 publications

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“…arx-7 encodes a subunit of the Arp2/3 complex, which is also known to be crucial for endocytic trafficking [61]. GGTB-1 is a homolog of human RABGGTB (Rab geranylgeranyltransferase β subunit), which presumably participates in the attachment of a geranylgeranyl group to the cysteine at the C-terminus of Rab [62].…”

Section: Plos Geneticsmentioning

confidence: 99%

An EHBP-1-SID-3-DYN-1 axis promotes membranous tubule fission during endocytic recycling

et al. 2020

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The ACK family tyrosine kinase SID-3 is involved in the endocytic uptake of double-stranded RNA. Here we identified SID-3 as a previously unappreciated recycling regulator in the Caenorhabditis elegans intestine. The RAB-10 effector EHBP-1 is required for the endosomal localization of SID-3. Accordingly, animals with loss of SID-3 phenocopied the recycling defects observed in ehbp-1 and rab-10 single mutants. Moreover, we detected sequential protein interactions between EHBP-1, SID-3, NCK-1, and DYN-1. In the absence of SID-3, DYN-1 failed to localize at tubular recycling endosomes, and membrane tubules breaking away from endosomes were mostly absent, suggesting that SID-3 acts synergistically with the downstream DYN-1 to promote endosomal tubule fission. In agreement with these observations, overexpression of DYN-1 significantly increased recycling transport in SID-3deficient cells. Finally, we noticed that loss of RAB-10 or EHBP-1 compromised feeding RNAi efficiency in multiple tissues, implicating basolateral recycling in the transport of RNA silencing signals. Taken together, our study demonstrated that in C. elegans intestinal epithelia, SID-3 acts downstream of EHBP-1 to direct fission of recycling endosomal tubules in concert with NCK-1 and DYN-1.

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Section: Plos Geneticsmentioning

confidence: 99%

An EHBP-1-SID-3-DYN-1 axis promotes membranous tubule fission during endocytic recycling

et al. 2020

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“…arx-7 encodes a subunit of Arp2/3 complex, which is known to be essential for endocytic trafficking (Duleh & Welch, 2010). GGTB-1 is a C. elegans homolog of human RABGGTB (Rab geranylgeranyltransferase b subunit) that presumably catalyzes the add-on of geranylgeranyl group to the C-terminal cysteines of Rab proteins (Gutkowska & Swiezewska, 2012).…”

Section: Ptrn-1 Is Required For Proper Actin Organization In C Elegamentioning

confidence: 99%

PTRN‐1/CAMSAPpromotesCYK‐1/formin‐dependent actin polymerization during endocytic recycling

et al. 2018

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Cargo sorting and membrane carrier initiation in recycling endosomes require appropriately coordinated actin dynamics. However, the mechanism underlying the regulation of actin organization during recycling transport remains elusive. Here we report that the loss of PTRN-1/CAMSAP stalled actin exchange and diminished the cytosolic actin structures. Furthermore, we found that PTRN-1 is required for the recycling of clathrin-independent cargo hTAC-GFP The N-terminal calponin homology (CH) domain and central coiled-coils (CC) region of PTRN-1 can synergistically sustain the flow of hTAC-GFP We identified CYK-1/formin as a binding partner of PTRN-1. The N-terminal GTPase-binding domain (GBD) of CYK-1 serves as the binding interface for the PTRN-1 CH domain. The presence of the PTRN-1 CH domain promoted CYK-1-mediated actin polymerization, which suggests that the PTRN-1-CH:CYK-1-GBD interaction efficiently relieves autoinhibitory interactions within CYK-1. As expected, the overexpression of the CYK-1 formin homology domain 2 (FH2) substantially restored actin structures and partially suppressed the hTAC-GFP overaccumulation phenotype in mutants. We conclude that the PTRN-1 CH domain is required to stimulate CYK-1 to facilitate actin dynamics during endocytic recycling.

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“…FTase and GGTaseI are heterodimers with one common subunit, and can occasionally modify the same sites. GGTaseII is structurally distinct and only modifies Rab proteins (>60 in mammals) at the C-terminal consensus sequence CXC, CC, or CCX (Gutkowska and Swiezewska, 2012). It works in concert with a third protein, Rab escort protein (REP), and typically transfers two geranylgeranyl groups.…”

Section: Overview Of Lipid Modifications Of Proteinmentioning

confidence: 99%

All about that fat: Lipid modification of proteins in Cryptococcus neoformans

Santiago-Tirado

Doering²

2016

J Microbiol.

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Lipid modification of proteins is a widespread, essential process whereby fatty acids, cholesterol, isoprenoids, phospholipids, or glycosylphospholipids are attached to polypeptides. These hydrophobic groups may affect protein structure, function, localization, and/or stability; as a consequence such modifications play critical regulatory roles in cellular systems. Recent advances in chemical biology and proteomics have allowed the profiling of modified proteins, enabling dissection of the functional consequences of lipid addition. The enzymes that mediate lipid modification are specific for both the lipid and protein substrates, and are conserved from fungi to humans. In this article we review these enzymes, their substrates, and the processes involved in eukaryotic lipid modification of proteins. We further focus on its occurrence in the fungal pathogen Cryptococcus neoformans, highlighting unique features that are both relevant for the biology of the organism and potentially important in the search for new therapies.

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Structure, regulation and cellular functions of Rab geranylgeranyl transferase and its cellular partner Rab Escort Protein

Cited by 13 publications

References 67 publications

An EHBP-1-SID-3-DYN-1 axis promotes membranous tubule fission during endocytic recycling

An EHBP-1-SID-3-DYN-1 axis promotes membranous tubule fission during endocytic recycling

PTRN‐1/CAMSAPpromotesCYK‐1/formin‐dependent actin polymerization during endocytic recycling

All about that fat: Lipid modification of proteins in Cryptococcus neoformans

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