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| 2. |
- Nilsson, Lars, et al.
(author)
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C. elegans TAT-6, a putative aminophospholipid translocase, is expressed in sujc cells in the hermaphrodite gonad
- 2021
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In: microPublication biology. - : Caltech Library. - 2578-9430.
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Journal article (peer-reviewed)abstract
- In healthy eukaryotic cells, the two leaflets that make up plasma membranes are highly asymmetric with respect to the lipids they contain. In both unicellular eukaryotes and metazoans, the asymmetry in the distribution of aminophospholipids is maintained by P4-family transmembrane ATPases, which catalyze the movement of selected phospholipids from the outer leaflet to the inner. C. elegans has six P4-family ATPases, TAT-1 - TAT-6. TAT-1 - TAT-5 are expressed in many tissues and cells. Here we report that, in contrast, TAT-6 is much less broadly expressed and that, within the somatic gonad, expression of TAT-6 reporters is restricted to the spermathecal-uterine core cell (sujc) cells.
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| 3. |
- Pu, Longjun, et al.
(author)
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Hypoxia induces food leaving in C. elegans
- 2023
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In: microPublication Biology. - : California Institute of Technology. - 2578-9430.
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Journal article (peer-reviewed)abstract
- Hypoxia alters eating behavior in different animals. In C. elegans, hypoxia induces a strong food leaving response. We found that this behavior was independent of the known O 2 response mechanisms including acute O2 sensation and HIF-1 signaling of chronic hypoxia response. Mutating egl-3 and egl-21, encoding the neuropeptide pro-protein convertase and carboxypeptidase, led to defects in hypoxia induced food leaving, suggesting that neuropeptidergic signaling was required for this response. However, we failed to identify any neuropeptide mutants that were severely defective in hypoxia induced food leaving, suggesting that multiple neuropeptides act redundantly to modulate this behavior.
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| 4. |
- Pu, Longjun, et al.
(author)
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Iterative editing of multiple genes using CRISPR/Cas9 in C. elegans
- 2023
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In: microPublication Biology. - : Caltech Library. - 2578-9430.
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Journal article (peer-reviewed)abstract
- Certain sets of genes are derived from gene duplication and share substantial sequence similarity in C. elegans, presenting a significant challenge in determining the specific roles of each gene and their collective impact on cellular processes. Here, we show that a collection of genes can be disrupted in a single animal via multiple rounds of CRISPR/Cas9 mediated genome editing. We found that up to three genes can be simultaneously disrupted in a single editing event with high efficiency. Our approach offers an opportunity to explore the genetic interaction and molecular underpinning of gene clusters with redundant function.
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| 5. |
- Rahmani, Shapour, et al.
(author)
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EGL-4 promotes turning behavior of C. elegans males during mating
- 2021
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In: microPublication biology. - : Caltech Library. - 2578-9430.
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Journal article (peer-reviewed)abstract
- During mating, C. elegans males whose tails have reached the head or tail of their intended mates are able to switch to scanning the other side by performing a turn during which the male's tail curls ventrally all the while keeping in contact with the hermaphrodite. The ability to execute turns efficiently is dependent upon serotonergic neurons in the posterior ventral nerve cord that stimulate diagonal muscles by activating a serotonin receptor, SER-1. Here we show that turning behavior is abnormal in males lacking a cGMP-dependent protein kinase, EGL-4. egl-4 mutant males are also resistant to ventral tail curling induced by exogenous serotonin.
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| 6. |
- Wang, Zuoneng, et al.
(author)
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CryoEM reveals BIN1 (isoform 8) does not bind to single actinfilaments in vitro
- 2021
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In: microPublication biology. - : Caltech Library. - 2578-9430.
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Journal article (other academic/artistic)abstract
- Cells change their appearance by a concerted action of the cytoskeleton and the plasma membrane. The machinery thatbends the membrane includes Bin/Amphiphysin/Rvs (BAR) domain proteins. Recently BAR domain proteins garneredattention as actin regulators, either by recruiting actin regulating proteins or through binding to actin directly. BIN1 (animportant protein in Alzheimer’s Disease, heart disease and cancer) is one of the few BAR proteins that bind to actindirectly. Here, we imaged a complex of BIN1 and actin with cryoEM. Our results reveal that BIN1 cannot be found onsingle actin filaments.
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