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Furthermore, some BAR domains have been found to bind to small GTPases, a class of intracellular molecular switches (Tarricone et al, 2001; Habermann, 2004); thus, their membrane association is directly linked to regulation of signal transduction and trafficking.
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In contrast to small GTPases, relatively little is known about the mechanisms mediating the localization of GTPases from the family of guanylate-binding proteins (GBPs).
Arfaptin-1 was reported to bind to curved membrane structures with its crescent shaped Bin/Amphiphysin/Rvs (BAR) domain., In addition to curved membranes, Arfaptin-1 also binds to activated small GTPases of the ARF family.
Related repeats to the LRRs are known to bind small GTPases of the Ras superfamily (Jou and Nelson, 1998; Kaibuchi et al, 1999).
The Mog1 protein binds to the small GTPase Ran that plays an important role in nuclear import.
β-karyopherins were originally identified based on their ability to bind the small GTPase Ran through an N-terminal binding domain [ 9].
A structural study on the closely related protein Arfaptin-2 has revealed that Arfaptins can cooperatively bind small GTPases of the ARF family and curved membranes.
GAPs are a family of regulatory proteins whose members can bind and activate small GTPases and others G proteins.
For example, PH domains in some guanine nucleotide-exchange factors (GEF) have been shown to bind directly to their cognate small GTPases (Rossman et al, 2002, 2003; Lu et al, 2004), and our data now show direct interaction between the APPL1 PH domain and Rab5.
Rev binds to the nuclear export protein Crm1 which in turn binds to Ran, a small GTPase that shuttles between the nucleus and the cytoplasm.
Their phospholipid composition changes (i.e., acquire phosphatidylinositol 3-phosphate) and they bind the small GTPase Rab5 and early endosomal antigen 1 (EEare, are tethered to microtubules and become classical early endosomes.
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