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  1. Article ; Online: Regulation and functions of membrane lipids: Insights from

    Koyiloth, Muhasin / Gummadi, Sathyanarayana N

    BBA advances

    2022  Volume 2, Page(s) 100043

    Abstract: ... ...

    Abstract The
    Language English
    Publishing date 2022-01-15
    Publishing country Netherlands
    Document type Journal Article ; Review
    ISSN 2667-1603
    ISSN (online) 2667-1603
    DOI 10.1016/j.bbadva.2022.100043
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Interaction of human phospholipid scramblase 1 with cholesterol via CRAC motif is essential for functional regulation and subcellular localization.

    Koyiloth, Muhasin / Gummadi, Sathyanarayana N

    International journal of biological macromolecules

    2022  Volume 209, Issue Pt A, Page(s) 850–857

    Abstract: Human phospholipid scramblase 1 (hPLSCR1) possesses a putative cholesterol binding CRAC (cholesterol interaction/recognition amino acid consensus) motif at the C-terminal. The CRAC motif of hPLSCR1 interacts with cholesterol with an energy of interaction ...

    Abstract Human phospholipid scramblase 1 (hPLSCR1) possesses a putative cholesterol binding CRAC (cholesterol interaction/recognition amino acid consensus) motif at the C-terminal. The CRAC motif of hPLSCR1 interacts with cholesterol with an energy of interaction -64.39 KJ mol
    MeSH term(s) Cell Membrane/metabolism ; Cholesterol/metabolism ; Humans ; Membrane Microdomains/metabolism ; Phospholipid Transfer Proteins/chemistry ; Phospholipid Transfer Proteins/genetics ; Phospholipid Transfer Proteins/metabolism
    Chemical Substances PLSCR1 protein, human ; Phospholipid Transfer Proteins ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2022-04-18
    Publishing country Netherlands
    Document type Journal Article
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2022.04.087
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Regulation and functions of membrane lipids: Insights from Caenorhabditis elegans

    Koyiloth, Muhasin / Gummadi, Sathyanarayana N.

    BBA advances. 2022, v. 2

    2022  

    Abstract: The Caenorhabditis elegans plasma membrane is composed of glycerophospholipids and sphingolipids with a small cholesterol. The C. elegans obtain the majority of the membrane lipids by modifying fatty acids present in the bacterial diet. The metabolic ... ...

    Abstract The Caenorhabditis elegans plasma membrane is composed of glycerophospholipids and sphingolipids with a small cholesterol. The C. elegans obtain the majority of the membrane lipids by modifying fatty acids present in the bacterial diet. The metabolic pathways of membrane lipid biosynthesis are well conserved across the animal kingdom. In C. elegans CDP-DAG and Kennedy pathway produce glycerophospholipids. Meanwhile, the sphingolipids are synthesized through a different pathway. They have evolved remarkably diverse mechanisms to maintain membrane lipid homeostasis. For instance, the lipid bilayer stress operates to accomplish homeostasis during any perturbance in the lipid composition. Meanwhile, the PAQR-2/IGLR-2 complex works with FLD-1 to balance unsaturated to saturated fatty acids to maintain membrane fluidity. The loss of membrane lipid homeostasis is observed in many human genetic and metabolic disorders. Since C. elegans conserved such genes and pathways, it can be used as a model organism.
    Keywords Caenorhabditis elegans ; biosynthesis ; cholesterol ; diet ; glycerophospholipids ; homeostasis ; humans ; lipid bilayers ; lipid composition ; membrane fluidity ; plasma membrane ; sphingolipids
    Language English
    Publishing place Elsevier B.V.
    Document type Article
    ISSN 2667-1603
    DOI 10.1016/j.bbadva.2022.100043
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  4. Article ; Online: Interaction of human phospholipid scramblase 1 with cholesterol via CRAC motif is essential for functional regulation and subcellular localization

    Koyiloth, Muhasin / Gummadi, Sathyanarayana N.

    International Journal of Biological Macromolecules. 2022 June, v. 209 p.850-857

    2022  

    Abstract: Human phospholipid scramblase 1 (hPLSCR1) possesses a putative cholesterol binding CRAC (cholesterol interaction/recognition amino acid consensus) motif at the C-terminal. The CRAC motif of hPLSCR1 interacts with cholesterol with an energy of interaction ...

    Abstract Human phospholipid scramblase 1 (hPLSCR1) possesses a putative cholesterol binding CRAC (cholesterol interaction/recognition amino acid consensus) motif at the C-terminal. The CRAC motif of hPLSCR1 interacts with cholesterol with an energy of interaction −64.39 KJ mol⁻¹. Since palmitoylated hPLSCR1 localizes to the cholesterol-rich lipid rafts, the interaction between hPLSCR1 and raft cholesterol is highly likely. The present study investigated the hPLSCR1-cholesterol interaction in plasma membrane via putative CRAC motif. hPLSCR1 remains at cholesterol-rich lipid rafts as long as they interact. This interaction is inhibited by mutations in the CRAC motif or cholesterol depletion. Thus, CRAC mutants I300D hPLSCR1 and ΔCRAC hPLSCR1 diffused to the cytoplasm and nucleus. Cholesterol depletion by methyl-β-cyclodextrin (MβCD) dose-dependently reduced cell viability in A549 cells. However, cholesterol depletion released 1.74 ± 0.12 times Ca²⁺ to the cytosol in A549 cells. Similarly, cholesterol depletion increased intracellular Ca²⁺ release by 1.81 ± 0.13 and 4.11 ± 0.19 times in RAJI cells expressing hPLSCR1 and ΔCRAC hPLSCR1, respectively. Moreover, the expression of hPLSCR1 and ΔCRAC hPLSCR1 increased apoptosis in RAJI cells by 21 ± 1.5% and 53.50 ± 4.40%, respectively. It was further increased to 43 ± 2.5% and 71.4 ± 1.4% upon cholesterol depletion. The current work links hPLSCR1 expression with cholesterol depletion, intracellular Ca²⁺ release, and induction of apoptosis.
    Keywords amino acids ; apoptosis ; calcium ; cell viability ; cholesterol ; cytosol ; energy ; humans ; phospholipids ; plasma membrane ; Methyl-β-cyclodextrin ; Intracellular calcium assay
    Language English
    Dates of publication 2022-06
    Size p. 850-857.
    Publishing place Elsevier B.V.
    Document type Article ; Online
    ZDB-ID 282732-3
    ISSN 1879-0003 ; 0141-8130
    ISSN (online) 1879-0003
    ISSN 0141-8130
    DOI 10.1016/j.ijbiomac.2022.04.087
    Database NAL-Catalogue (AGRICOLA)

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  5. Article ; Online: Cholesterol interaction attenuates scramblase activity of SCRM-1 in the artificial membrane.

    Koyiloth, Muhasin / Gummadi, Sathyanarayana N

    Biochimica et biophysica acta. Biomembranes

    2021  Volume 1863, Issue 9, Page(s) 183548

    Abstract: Phospholipid (PL) scramblases are single-pass transmembrane protein mediating bidirectional PL translocation. Previously in silico analysis of human PL scramblases, predicted the presence of an uncharacterized cholesterol-binding domain spanning partly ... ...

    Abstract Phospholipid (PL) scramblases are single-pass transmembrane protein mediating bidirectional PL translocation. Previously in silico analysis of human PL scramblases, predicted the presence of an uncharacterized cholesterol-binding domain spanning partly in the transmembrane helix as well as in the adjacent extracellular coil. This domain was found to be universally conserved in diverse organisms like Caenorhabditis elegans. In this study, we investigated the saturable cholesterol-binding domain of SCRM-1 using fluorescence sterol binding assay, Stern-Volmer quenching, Förster resonance energy transfer, and CD spectroscopy. We observed high-affinity interaction between cholesterol and SCRM-1. Our results support a previous report, which showed that the cholesterol ordering effect reduced the scramblase activity of hPLSCR1. Considering the presence of a high-affinity binding sequence, we propose that the reduction in activity could partly be due to the cholesterol binding. To validate this, we generated a C-terminal helix (CTH) deletion construct (∆CTH SCRM-1) and a point mutation in the putative cholesterol-binding domain I273D SCRM-1. Deletion construct greatly reduced cholesterol affinity along with loss of scramblase activity. In contrast to this, I273D SCRM-1 retained scrambling activity in proteoliposomes containing ~30 mol% cholesterol but lost sterol binding ability. These results suggest that C-terminal helix is crucial for membrane insertion and in the lipid bilayer the scrambling activity of SCRM-1 is modulated through its interaction with cholesterol.
    MeSH term(s) Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/metabolism ; Cholesterol/chemistry ; Cholesterol/metabolism ; Humans ; Membranes, Artificial ; Phospholipid Transfer Proteins/chemistry ; Phospholipid Transfer Proteins/metabolism
    Chemical Substances Caenorhabditis elegans Proteins ; Membranes, Artificial ; Phospholipid Transfer Proteins ; SCRM-1 protein, C elegans ; Cholesterol (97C5T2UQ7J)
    Language English
    Publishing date 2021-01-06
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 60-7
    ISSN 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    ISSN (online) 1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
    ISSN 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
    DOI 10.1016/j.bbamem.2020.183548
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Molecular cloning and biochemical characterization of the phospholipid scramblase SCRM-1 from Caenorhabditis elegans.

    Koyiloth, Muhasin / Gummadi, Sathyanarayana N

    European biophysics journal : EBJ

    2020  Volume 49, Issue 2, Page(s) 163–173

    Abstract: In this study, the SCRM-1 gene from Caenorhabditis elegans was cloned and overexpressed in E. coli to study the biochemical properties of scramblase. This is the first report showing that this scramblase from C. elegans possesses a ... ...

    Abstract In this study, the SCRM-1 gene from Caenorhabditis elegans was cloned and overexpressed in E. coli to study the biochemical properties of scramblase. This is the first report showing that this scramblase from C. elegans possesses a Ca
    MeSH term(s) Amino Acid Motifs ; Animals ; Binding Sites ; Caenorhabditis elegans/enzymology ; Caenorhabditis elegans Proteins/genetics ; Caenorhabditis elegans Proteins/metabolism ; Calcium/chemistry ; Calcium/metabolism ; Carbocyanines/chemistry ; Cell Membrane/metabolism ; Cloning, Molecular ; Escherichia coli/metabolism ; Liposomes/chemistry ; Mutation ; Phospholipid Transfer Proteins/genetics ; Phospholipid Transfer Proteins/metabolism ; Phospholipids/chemistry ; Plasmids/metabolism ; Point Mutation ; Protein Domains ; Terbium/chemistry ; Time Factors ; Tryptophan/chemistry
    Chemical Substances Caenorhabditis elegans Proteins ; Carbocyanines ; Liposomes ; Phospholipid Transfer Proteins ; Phospholipids ; SCRM-1 protein, C elegans ; Terbium (06SSF7P179) ; Tryptophan (8DUH1N11BX) ; Calcium (SY7Q814VUP)
    Language English
    Publishing date 2020-02-04
    Publishing country Germany
    Document type Journal Article
    ZDB-ID 283671-3
    ISSN 1432-1017 ; 0175-7571
    ISSN (online) 1432-1017
    ISSN 0175-7571
    DOI 10.1007/s00249-020-01423-2
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    Zs.A 1121: Show issues Location:
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  7. Article ; Online: Activin E is a transforming growth factor β ligand that signals specifically through activin receptor-like kinase 7.

    Vestal, Kylie A / Kattamuri, Chandramohan / Koyiloth, Muhasin / Ongaro, Luisina / Howard, James A / Deaton, Aimee M / Ticau, Simina / Dubey, Aditi / Bernard, Daniel J / Thompson, Thomas B

    The Biochemical journal

    2024  Volume 481, Issue 7, Page(s) 547–564

    Abstract: Activins are one of the three distinct subclasses within the greater Transforming growth factor β (TGFβ) superfamily. First discovered for their critical roles in reproductive biology, activins have since been shown to alter cellular differentiation and ... ...

    Abstract Activins are one of the three distinct subclasses within the greater Transforming growth factor β (TGFβ) superfamily. First discovered for their critical roles in reproductive biology, activins have since been shown to alter cellular differentiation and proliferation. At present, members of the activin subclass include activin A (ActA), ActB, ActC, ActE, and the more distant members myostatin and GDF11. While the biological roles and signaling mechanisms of most activins class members have been well-studied, the signaling potential of ActE has remained largely unknown. Here, we characterized the signaling capacity of homodimeric ActE. Molecular modeling of the ligand:receptor complexes showed that ActC and ActE shared high similarity in both the type I and type II receptor binding epitopes. ActE signaled specifically through ALK7, utilized the canonical activin type II receptors, ActRIIA and ActRIIB, and was resistant to the extracellular antagonists follistatin and WFIKKN. In mature murine adipocytes, ActE invoked a SMAD2/3 response via ALK7, like ActC. Collectively, our results establish ActE as a specific signaling ligand which activates the type I receptor, ALK7.
    MeSH term(s) Mice ; Animals ; Transforming Growth Factor beta/metabolism ; Ligands ; Activin Receptors/genetics ; Activin Receptors/metabolism ; Carrier Proteins ; Activins/metabolism
    Chemical Substances Transforming Growth Factor beta ; Ligands ; Activin Receptors (EC 2.7.11.30) ; Carrier Proteins ; Activins (104625-48-1)
    Language English
    Publishing date 2024-03-27
    Publishing country England
    Document type Journal Article
    ZDB-ID 2969-5
    ISSN 1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
    ISSN (online) 1470-8728
    ISSN 0006-2936 ; 0306-3275 ; 0264-6021
    DOI 10.1042/BCJ20230404
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  8. Article: Activin E is a TGFβ ligand that signals specifically through activin receptor-like kinase 7.

    Vestal, Kylie A / Kattamuri, Chandramohan / Koyiloth, Muhasin / Ongaro, Luisina / Howard, James A / Deaton, Aimee / Ticau, Simina / Dubey, Aditi / Bernard, Daniel J / Thompson, Thomas B

    bioRxiv : the preprint server for biology

    2023  

    Abstract: Activins are one of the three distinct subclasses within the greater Transforming Growth Factor β (TGFβ) superfamily. First discovered for their critical roles in reproductive biology, activins have since been shown to alter cellular differentiation and ... ...

    Abstract Activins are one of the three distinct subclasses within the greater Transforming Growth Factor β (TGFβ) superfamily. First discovered for their critical roles in reproductive biology, activins have since been shown to alter cellular differentiation and proliferation. At present, members of the activin subclass include activin A (ActA), ActB, ActC, ActE, and the more distant members myostatin and GDF11. While the biological roles and signaling mechanisms of most activins class members have been well-studied, the signaling potential of ActE has remained largely unknown. Here, we characterized the signaling capacity of homodimeric ActE. Molecular modeling of the ligand:receptor complexes showed that ActC and ActE shared high similarity in both the type I and type II receptor binding epitopes. ActE signaled specifically through ALK7, utilized the canonical activin type II receptors, ActRIIA and ActRIIB, and was resistant to the extracellular antagonists follistatin and WFIKKN. In mature murine adipocytes, ActE invoked a SMAD2/3 response via ALK7, similar to ActC. Collectively, our results establish ActE as an ALK7 ligand, thereby providing a link between genetic and
    Language English
    Publishing date 2023-09-25
    Publishing country United States
    Document type Preprint
    DOI 10.1101/2023.09.25.559288
    Database MEDical Literature Analysis and Retrieval System OnLINE

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