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However, in certain cohorts, many individuals test positive for IgA aPL alone or with other aPL [1] [18].
Constructs containing papl-1::apl-1ΔYENPTY::gfp, papl-1::apapl-1T658A::gfp, and papl-1 T658E papl-1 T658Eerated from the origfpal papl-1::apl-1::gfp full length construct using site-directed mutagenesis to introduce the individual mutations.
Worms with apl-1 knocked-down share the loose cuticle and internal vacuolization phenotypes of apl-1 tm385 apl-1 tm385hibit these phenotypes L1ser in development.
To determine the expression pattern of apl-1, transgenic worms were generated expressing an apl-1 gfp apl-1 gfptein driven by the endogenous apl-1 promoter.
Previous genetic rescue studies showed that the full length APL-1, the N-terminal sequences of APL-1, as well as the non-overlapping E1 or E2 fragments of APL-1 were sufficient to rescue apl-1 null lethality [8].
The ability of UNC-108 to alter the localization of APL-1 points to a novel process by which APL-1 is regulated in the cell.
Our results reveal novel insights into the intracellular trafficking of APL-1 and we report a functional role for APL-1 in synaptic transmission.
To determine whether APL-1 was also present in RAB-5 compartments in the worm we generated strains co-expressing APL-1 GFP APL-1 GFPy::Rand5.
Furthermore, different domains in APL-1 and APPL are required for their respective functions.
We found that apl-1 RNAi treated worms exhibited hypersensitivity to aldicarb (Figure 2A, B).
In this study, we use C. elegans to investigate the normal functional role of APL-1.
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