Lela Jackson

ORCID: 0000-0003-1779-0806
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About
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Research Areas
  • RNA Research and Splicing
  • Protein Kinase Regulation and GTPase Signaling
  • Endoplasmic Reticulum Stress and Disease
  • Cell death mechanisms and regulation
  • RNA regulation and disease
  • RNA Interference and Gene Delivery
  • Caveolin-1 and cellular processes
  • MicroRNA in disease regulation
  • Cellular transport and secretion
  • RNA and protein synthesis mechanisms
  • Signaling Pathways in Disease
  • Ichthyology and Marine Biology
  • Alzheimer's disease research and treatments
  • Viral Infectious Diseases and Gene Expression in Insects
  • NF-κB Signaling Pathways
  • Mechanisms of cancer metastasis
  • Receptor Mechanisms and Signaling
  • Glycosylation and Glycoproteins Research
  • Neuroscience and Neuropharmacology Research
  • Cephalopods and Marine Biology
  • Photoreceptor and optogenetics research

Worcester Polytechnic Institute
2019-2022

University of North Texas Health Science Center
2003

University of North Texas
2003

Stimulation of Gα q -coupled GPCRs releases PLCβ1 from stress granule–associated proteins, enabling their aggregation.

10.1126/scisignal.aav1012 article EN Science Signaling 2021-10-19

Phospholipase Cβ1 is activated by Gαq to generate calcium signals in response hormones and neurotransmitters. Besides carrying out this plasma membrane function, PLCβ1 has a cytosolic population that helps drive the differentiation of PC12 cells inhibiting nuclease promotes RNA-induced silencing (C3PO). Here, we show down-regulating or reducing its activating localize it returns differentiated SK-N-SH an undifferentiated state. In state, have spherical morphology, resume proliferation,...

10.1096/fj.201902668r article EN The FASEB Journal 2020-08-06

Abstract The Gαq/phospholipase Cβ1 (PLCβ1) signaling system mediates calcium responses from hormones and neurotransmitters. While PLCβ1 functions on the plasma membrane, there is an atypical cytosolic population that binds Argonaute 2 (Ago2) other proteins associated with stress granules preventing their aggregation. Activation of Gαq relocalizes to releasing bound proteins, promoting formation granules. Here, we have characterized Ago2 activation in differentiated PC12 cells, which a robust...

10.1038/s41598-022-12737-w article EN cc-by Scientific Reports 2022-05-24

10.1038/135792a0 article EN Nature 1935-05-01

During adverse conditions, mammalian cells regulate protein production by sequestering the translational machinery in membrane-less organelles known as stress granules. Here, we found that activation of G subunit Gαq promoted formation particles contained granule proteins through a mechanism linked to presence phospholipase Cβ1 (PLCβ1) cytosol. In experiments with PC12 and A10 cells, showed under basal cytosolic PLCβ1 bound associated proteins, including PABPC1, eIF5A, Ago2. Knockdown siRNA...

10.1101/521369 preprint EN cc-by-nd bioRxiv (Cold Spring Harbor Laboratory) 2019-01-15

During adverse environmental conditions, mammalian cells regulate protein production by sequestering the translation machinery in membraneless organelles (i.e. stress granules) whose formation is carefully regulated. In this study, we show a direct connection between G signaling and granule through phospholipase Cβ (PLCβ). cells, PLCβ localizes to both cytoplasm plasma membrane. We find that major population of cytosolic binds proteins; specifically, eIF5A Ago2, RNA‐induced silencing...

10.1096/fasebj.2019.33.1_supplement.477.11 article EN The FASEB Journal 2019-04-01

10.1016/j.bpj.2018.11.732 article EN publisher-specific-oa Biophysical Journal 2019-02-01

ABSTRACT Phospholipase Cβ1 is activated by Gαq to generate calcium signals in response hormones and neurotransmitters, found at high levels mammalian neuronal tissue. Besides carrying out this key plasma membrane function, PLCβ1 has a cytosolic population that helps, part, drive the differentiation of PC12 cells inhibiting nuclease promotes RNA-induced silencing (C3PO). Here, we show down-regulating or reducing its activating it membrane, returns differentiated an undifferentiated state. In...

10.1101/2020.01.06.896530 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-01-06

10.1016/j.bpj.2021.11.1706 article EN publisher-specific-oa Biophysical Journal 2022-02-01

Abstract Hormones and neurotransmitters can activate the Gαq / phospholipase Cβ1 (PLCβ1) signaling system eliciting cellular calcium responses. Aside from plasma membrane, PLCβ1 has a cytosolic population that binds stress granule associated proteins preventing their aggregation, activation of shifts to membrane releasing bound promoting formation granules. The impact granules formed upon routine protein is unknown. Here, we have characterized Ago2 in response neurotransmitter cultured PC12...

10.21203/rs.3.rs-1269940/v1 preprint EN cc-by Research Square (Research Square) 2022-01-27

Abstract Hormones and neurotransmitters can activate the Gαq / phospholipase Cβ1 (PLCβ1) signaling system eliciting cellular calcium responses. PLCβ1 also prevents aggregation of ribosomal RNA proteins into stress granules, which are halted translation complexes that form in response to stress. Activation promotes PLCβ1association releasing bound promoting formation granules. However, impact granules formed from routine protein is unknown. Here, we have characterized Ago2 activation a...

10.21203/rs.3.rs-960537/v1 preprint EN cc-by Research Square (Research Square) 2021-10-26
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