PITPNM1

Last update 23 Jan 2025

Basic Info

Synonyms

DRES9, Drosophila retinal degeneration B homolog, Membrane-associated phosphatidylinositol transfer protein 1

+ [12]

Introduction

Catalyzes the transfer of phosphatidylinositol (PI) between membranes (PubMed:22822086, PubMed:10531358). Binds PI, phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (PubMed:22822086). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (PubMed:11909959). Necessary for normal completion of cytokinesis (PubMed:15125835). Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus (PubMed:15723057). Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus (PubMed:15545272). Required for protein export from the endoplasmic reticulum and the Golgi (PubMed:15723057). Binds calcium ions (PubMed:10022914).

100 Clinical Results associated with PITPNM1

100 Translational Medicine associated with PITPNM1

0 Patents (Medical) associated with PITPNM1

188

Literatures (Medical) associated with PITPNM1

01 Jun 2024·Life Science Alliance

A genetic screen to uncover mechanisms underlying lipid transfer protein function at membrane contact sites

Article

Author: Bhattacharya, Subhodeep ; Mishra, Shirish ; Raghu, Padinjat ; Nath, Vaisaly R ; Chandel, Shabnam ; Manoj, Tejaswini ; Krishnan, Harini ; Martinet, Arthur ; Alpy, Fabien ; Di Mattia, Thomas ; Manohar, Vaishnavi ; Chimata, Prasanth ; Wendling, Corinne ; Hegde, Nidhi

Lipid transfer proteins mediate the transfer of lipids between organelle membranes, and the loss of function of these proteins has been linked to neurodegeneration. However, the mechanism by which loss of lipid transfer activity leads to neurodegeneration is not understood. InDrosophilaphotoreceptors, depletion of retinal degeneration B (RDGB), a phosphatidylinositol transfer protein, leads to defective phototransduction and retinal degeneration, but the mechanism by which loss of this activity leads to retinal degeneration is not understood. RDGB is localized to membrane contact sites through the interaction of its FFAT motif with the ER integral protein VAP. To identify regulators of RDGB function in vivo, we depleted more than 300 VAP-interacting proteins and identified a set of 52 suppressors ofrdgB. The molecular identity of these suppressors indicates a role of novel lipids in regulating RDGB function and of transcriptional and ubiquitination processes in mediating retinal degeneration inrdgB9. The human homologs of several of these molecules have been implicated in neurodevelopmental diseases underscoring the importance of VAP-mediated processes in these disorders.

29 Dec 2023·Journal of Biomolecular Structure and Dynamics

Structural organization of RDGB (retinal degeneration B), a multi-domain lipid transfer protein: a molecular modelling and simulation based approach

Article

Author: Raghu, Padinjat ; Krishnan, Harini ; Mishra, Shirish ; Basak, Bishal ; Nath, Vaisaly R

Lipid transfer proteins (LTPs) that shuttle lipids at membrane contact sites (MCS) play an important role in maintaining cellular homeostasis. One such important LTP is the Retinal Degeneration B (RDGB) protein. RDGB is localized at the MCS formed between the endoplasmic reticulum (ER) and the apical plasma membrane (PM) in Drosophila photoreceptors where it transfers phosphatidylinositol (PI) during G-protein coupled phospholipase C signalling. Previously, the C-terminal domains of RDGB have been shown to be essential for its function and accurate localization. In this study, using in-silico integrative modelling we predict the structure of entire RDGB protein in complex with the ER membrane protein VAP. The structure of RDGB has then been used to decipher the structural features of the protein important for its orientation at the contact site. Using this structure, we identify two lysine residues in the C-terminal helix of the LNS2 domain important for interaction with the PM. Using molecular docking, we also identify an unstructured region USR1, immediately c-terminal to the PITP domain that is important for the interaction of RDGB with VAP. Overall the 10.06 nm length of the predicted RDGB-VAP complex spans the distance between the PM and ER and is consistent with the cytoplasmic gap between the ER and PM measured by transmission electron microscopy in photoreceptors. Overall our model explains the topology of the RDGB-VAP complex at this ER-PM contact site and paves the way for analysis of lipid transfer function in this setting.Communicated by Ramaswamy H. Sarma.

01 Oct 2023·The International Journal of Mycobacteriology

Antibody Reactivity to Mycobacterium tuberculosis-specific Regions of Differences 1 and Regions of Differences 9 Proteins and Peptides in Rabbits, Mice, and Humans

Article

Author: Mustafa, A. S. ; Al-Attiyah, R. ; Hanif, Shumaila N. M.

Background:The major antigens encoded by Mycobacterium tuberculosis-specific genomic regions of differences (RDs) could be useful in the development of new vaccines and/or diagnostic reagents using T-cell and/or antibody assays. In particular, RD1 proteins PE35, PPE68, ESXA, ESXB, and RD9 protein ESXV and their peptides have been identified as major T-cell antigens. However, little is known about their antibody reactivities in different mammalian species. This study aims to determine the antigen-specific antibody reactivities to the above antigens and their peptides in three different mammalian species, i.e., rabbits, mice, and humans.Methods:Sera were obtained from (i) rabbits immunized with purified recombinant proteins PE35, PPE68, ESXA, ESXB, and ESXV; (ii) mice immunized with recombinant DNA vaccine constructs of pUMVC6 and pUMVC7 containing RD1 and RD9 genes; and (iii) tuberculosis (TB) patients and healthy humans. Enzyme-linked immunosorbent assays (ELISAs) were performed with the sera to determine the antibody reactivity to purified recombinant proteins, peptide pools, and individual peptides of RD1 and RD9 proteins.Results:The ELISA results with sera from rabbits immunized with pure recombinant proteins showed positive antibody reactivity with all of the immunizing proteins and their synthetic peptide pools. Testing of the sera with individual peptides showed positive antibody reactivity with PE35 peptides P1 (aa 1–25), P2 (aa 16–40), P5 (aa 61–85), and P6 (aa 76–99); PPE68 peptides P9 (aa 121–145), P11 (aa 151–175), P14 (aa 196–220), P22 (aa 316–340), P23 (aa 331–355), and P24 (aa 346–371); all peptides (P1 to P6) of ESXA and ESXB; and ESXV peptides P1 (aa 1–25), P2 (aa 16–40), P3 (aa 31–55), P5 (aa 61–85), and P6 (aa 76–94). The sera from mice immunized with DNA vaccine constructs showed antibody reactivity to all proteins and the peptide P6 (aa 76–99) of PE35 and peptides P19 (aa 271–295) and P24 (aa 346–371) of PPE68. In humans, the peptides P11 (aa 151–175), P14 (aa 196–220), P22 (aa 316–340), P23 (aa 331–355), and P24 (aa 346–371) of PPE68 and the peptides P4 (aa 46–70), P5 (aa 61–85), and P6 (aa 76–94) of ESXV showed positive reactivity with sera from TB patients and healthy controls.Conclusion:The results demonstrate the presence of several antibody epitopes in each protein, but variations in the epitopes recognized were observed among mice, rabbits, and humans, which could be due to mammalian species differences and/or mode of antigen delivery.

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PITPNM1

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