Abstrakt interacts with and regulates the expression of sorting nexin-2
Protein sorting through vesicular compartments is highly regulated to maintain the integrity and signaling of intracellular organelles in eukaryotic cells. Sorting Nexin‐2 (SNX2) is involved in protein sorting in the trans‐Golgi network, endosome, and/or lysosome compartments, with loss of function...
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| Published in | Journal of cellular physiology Vol. 204; no. 1; pp. 210 - 218 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
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01.07.2005
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| Abstract | Protein sorting through vesicular compartments is highly regulated to maintain the integrity and signaling of intracellular organelles in eukaryotic cells. Sorting Nexin‐2 (SNX2) is involved in protein sorting in the trans‐Golgi network, endosome, and/or lysosome compartments, with loss of function leading to defect in protein sorting and stress on organelles. To investigate the function of SNX2, we have identified the DEAD‐box helicase Abstrakt (Abs) as an SNX2‐interacting protein. The N‐terminal domain of Abs interacts with the phox homology (PX) domain of SNX2 suggesting that PX domains may also participate in protein–protein interaction. Interestingly, both proteins undergo nucleocytoplasmic shuttling, and this process is responsive to serum withdrawal for Abs. Finally, expression of Abs reduced the cellular expression of SNX2 without altering its steady state mRNA levels. This unexpected interaction provides a novel mechanism whereby expression of proteins involved in membrane trafficking could be regulated by an RNA helicase. © 2005 Wiley‐Liss, Inc. |
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| AbstractList | Protein sorting through vesicular compartments is highly regulated to maintain the integrity and signaling of intracellular organelles in eukaryotic cells. Sorting Nexin‐2 (SNX2) is involved in protein sorting in the trans‐Golgi network, endosome, and/or lysosome compartments, with loss of function leading to defect in protein sorting and stress on organelles. To investigate the function of SNX2, we have identified the DEAD‐box helicase Abstrakt (Abs) as an SNX2‐interacting protein. The N‐terminal domain of Abs interacts with the phox homology (PX) domain of SNX2 suggesting that PX domains may also participate in protein–protein interaction. Interestingly, both proteins undergo nucleocytoplasmic shuttling, and this process is responsive to serum withdrawal for Abs. Finally, expression of Abs reduced the cellular expression of SNX2 without altering its steady state mRNA levels. This unexpected interaction provides a novel mechanism whereby expression of proteins involved in membrane trafficking could be regulated by an RNA helicase. © 2005 Wiley‐Liss, Inc. Protein sorting through vesicular compartments is highly regulated to maintain the integrity and signaling of intracellular organelles in eukaryotic cells. Sorting Nexin-2 (SNX2) is involved in protein sorting in the trans-Golgi network, endosome, and/or lysosome compartments, with loss of function leading to defect in protein sorting and stress on organelles. To investigate the function of SNX2, we have identified the DEAD-box helicase Abstrakt (Abs) as an SNX2-interacting protein. The N-terminal domain of Abs interacts with the phox homology (PX) domain of SNX2 suggesting that PX domains may also participate in protein-protein interaction. Interestingly, both proteins undergo nucleocytoplasmic shuttling, and this process is responsive to serum withdrawal for Abs. Finally, expression of Abs reduced the cellular expression of SNX2 without altering its steady state mRNA levels. This unexpected interaction provides a novel mechanism whereby expression of proteins involved in membrane trafficking could be regulated by an RNA helicase. Protein sorting through vesicular compartments is highly regulated to maintain the integrity and signaling of intracellular organelles in eukaryotic cells. Sorting Nexin-2 (SNX2) is involved in protein sorting in the trans-Golgi network, endosome, and/or lysosome compartments, with loss of function leading to defect in protein sorting and stress on organelles. To investigate the function of SNX2, we have identified the DEAD-box helicase Abstrakt (Abs) as an SNX2-interacting protein. The N-terminal domain of Abs interacts with the phox homology (PX) domain of SNX2 suggesting that PX domains may also participate in protein-protein interaction. Interestingly, both proteins undergo nucleocytoplasmic shuttling, and this process is responsive to serum withdrawal for Abs. Finally, expression of Abs reduced the cellular expression of SNX2 without altering its steady state mRNA levels. This unexpected interaction provides a novel mechanism whereby expression of proteins involved in membrane trafficking could be regulated by an RNA helicase.Protein sorting through vesicular compartments is highly regulated to maintain the integrity and signaling of intracellular organelles in eukaryotic cells. Sorting Nexin-2 (SNX2) is involved in protein sorting in the trans-Golgi network, endosome, and/or lysosome compartments, with loss of function leading to defect in protein sorting and stress on organelles. To investigate the function of SNX2, we have identified the DEAD-box helicase Abstrakt (Abs) as an SNX2-interacting protein. The N-terminal domain of Abs interacts with the phox homology (PX) domain of SNX2 suggesting that PX domains may also participate in protein-protein interaction. Interestingly, both proteins undergo nucleocytoplasmic shuttling, and this process is responsive to serum withdrawal for Abs. Finally, expression of Abs reduced the cellular expression of SNX2 without altering its steady state mRNA levels. This unexpected interaction provides a novel mechanism whereby expression of proteins involved in membrane trafficking could be regulated by an RNA helicase. |
| Author | Abdul-Ghani, Mohammad Ngsee, Johnny K. Hartman, Kristin L. |
| Author_xml | – sequence: 1 givenname: Mohammad surname: Abdul-Ghani fullname: Abdul-Ghani, Mohammad organization: Ottawa Health Research Institute, Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario, Canada – sequence: 2 givenname: Kristin L. surname: Hartman fullname: Hartman, Kristin L. organization: Ottawa Health Research Institute, Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario, Canada – sequence: 3 givenname: Johnny K. surname: Ngsee fullname: Ngsee, Johnny K. email: jngsee@ohri.ca organization: Ottawa Health Research Institute, Cellular and Molecular Medicine, University of Ottawa, Ottawa, Ontario, Canada |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/15690390$$D View this record in MEDLINE/PubMed |
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J Cell Biol 165(1): 111-122. 2004; 165 1997; 272 2002; 13 2002; 277 2002; 99 1999; 24 2002; 3 1975; 254 2000; 91 2003; 278 2001; 506 1998; 273 1997; 8 1999; 9 1998; 1404 1998; 18 2004; 116 2001; 294 2001; 153 2000; 149 2004; 14 2000; 11 2004; 13 1996; 272 1996; 271 1997; 17 2003; 4 2003; 26 2001; 3 2001; 11 1985; 38 1998; 33 1998; 142 e_1_2_6_32_1 e_1_2_6_10_1 e_1_2_6_31_1 e_1_2_6_30_1 e_1_2_6_19_1 e_1_2_6_13_1 e_1_2_6_36_1 e_1_2_6_14_1 e_1_2_6_35_1 e_1_2_6_11_1 e_1_2_6_34_1 e_1_2_6_12_1 e_1_2_6_33_1 e_1_2_6_17_1 e_1_2_6_18_1 e_1_2_6_15_1 e_1_2_6_38_1 e_1_2_6_16_1 e_1_2_6_37_1 e_1_2_6_21_1 e_1_2_6_20_1 Peter BJ (e_1_2_6_28_1) 2003; 26 e_1_2_6_9_1 e_1_2_6_8_1 e_1_2_6_5_1 e_1_2_6_4_1 e_1_2_6_7_1 e_1_2_6_6_1 e_1_2_6_25_1 e_1_2_6_24_1 e_1_2_6_3_1 e_1_2_6_23_1 e_1_2_6_2_1 e_1_2_6_22_1 e_1_2_6_29_1 e_1_2_6_27_1 e_1_2_6_26_1 |
| References_xml | – reference: Linder P, Stutz F. 2001. mRNA export: Travelling with DEAD box proteins. Curr Biol 11(23): R961-963. – reference: Miaczynska M, Christoforidis S, Giner A, Shevchenko A, Uttenweiler-Joseph S, Habermann B, Wilm M, Parton RG, Zerial M. 2004. APPL proteins link Rab5 to nuclear signal transduction via an endosomal compartment. Cell 116(3): 445-456. – reference: Paine PL, Moore LC, Horowitz SB. 1975. Nuclear envelope permeability. Nature 254(5496): 109-114. – reference: Worby CA, Dixon JE. 2002. Sorting out the cellular functions of sorting nexins. Nat Rev Mol Cell Biol 3(12): 919-931. – reference: Kawamura H, Tomozoe Y, Akagi T, Kamei D, Ochiai M, Yamada M. 2002. Identification of the nucleocytoplasmic shuttling sequence of heterogeneous nuclear ribonucleoprotein D-like protein JKTBP and its interaction with mRNA. J Biol Chem 277(4): 2732-2739. – reference: Horazdovsky BF, Davies BA, Seaman MN, McLaughlin SA, Yoon S, Emr SD. 1997. 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| SubjectTerms | Animals Carrier Proteins - chemistry Carrier Proteins - genetics Carrier Proteins - metabolism Cell Nucleus - metabolism CHO Cells Cricetinae Culture Media, Serum-Free - pharmacology Cytoplasm - metabolism DEAD-box RNA Helicases Gene Expression Humans Protein Structure, Tertiary Protein Transport - physiology RNA Helicases - chemistry RNA Helicases - genetics RNA Helicases - metabolism RNA, Messenger - metabolism Vesicular Transport Proteins - chemistry Vesicular Transport Proteins - genetics Vesicular Transport Proteins - metabolism |
| Title | Abstrakt interacts with and regulates the expression of sorting nexin-2 |
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