Cotranslational Integration and Initial Sorting at the Endoplasmic Reticulum Translocon of Proteins Destined for the Inner Nuclear Membrane
The current diffusion-retention model for protein trafficking to the inner nuclear membrane (INM) proposes that INM proteins diffuse laterally from the membrane of the endoplasmic reticulum into the INM and are then retained in the INM by binding to nuclear proteins or DNA. Because some data indicat...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2004-08, Vol.101 (34), p.12537-12542 |
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| creator | Saksena, Suraj Shao, Yuanlong Braunagel, Sharon C. Summers, Max D. Johnson, Arthur E. |
| description | The current diffusion-retention model for protein trafficking to the inner nuclear membrane (INM) proposes that INM proteins diffuse laterally from the membrane of the endoplasmic reticulum into the INM and are then retained in the INM by binding to nuclear proteins or DNA. Because some data indicate that the sorting of baculovirus envelope proteins to the INM is protein-mediated, we have examined the early stages of INM protein integration and sorting by using photocrosslinking. Both viral and host INM-directed proteins were integrated cotranslationally through the endoplasmic reticulum translocon, and their nonrandom photocrosslinking to two translocon proteins, Sec61α and translocating chain-associated membrane protein (TRAM), revealed that the first transmembrane sequence (TMS) of each viral and host INM-directed protein occupied a very similar location within the translocon. Because few TMSs of non-INM-directed membrane proteins photocrosslink to TRAM, it seems that the INM-directed TMSs occupy different sites within the translocon than do non-INM-directed TMSs. The distinct proximities of translocon components to INM-directed TMSs strongly suggest that such TMSs are recognized and initially sorted within the translocon. Taken together, these data indicate that membrane protein sorting to the INM is an active process involving specific nonnuclear proteins. |
| doi_str_mv | 10.1073/pnas.0404934101 |
| format | Article |
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Because some data indicate that the sorting of baculovirus envelope proteins to the INM is protein-mediated, we have examined the early stages of INM protein integration and sorting by using photocrosslinking. Both viral and host INM-directed proteins were integrated cotranslationally through the endoplasmic reticulum translocon, and their nonrandom photocrosslinking to two translocon proteins, Sec61α and translocating chain-associated membrane protein (TRAM), revealed that the first transmembrane sequence (TMS) of each viral and host INM-directed protein occupied a very similar location within the translocon. Because few TMSs of non-INM-directed membrane proteins photocrosslink to TRAM, it seems that the INM-directed TMSs occupy different sites within the translocon than do non-INM-directed TMSs. The distinct proximities of translocon components to INM-directed TMSs strongly suggest that such TMSs are recognized and initially sorted within the translocon. 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| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2004-08, Vol.101 (34), p.12537-12542 |
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| source | MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry; JSTOR |
| subjects | Amino Acid Sequence Amino acids Animals Baculovirus Biological Sciences Cell membranes Cellular biology Codons Cross-Linking Reagents - metabolism Crosslinking Diffusion Dogs Endoplasmic Reticulum - metabolism Membrane Glycoproteins - metabolism Membrane proteins Membrane Proteins - metabolism Membranes Messenger RNA Microsomes Molecular Sequence Data Nuclear Envelope - metabolism Nuclear membrane Protein Biosynthesis Protein Transport Proteins Sequence Alignment Trolley cars Viral Proteins - metabolism |
| title | Cotranslational Integration and Initial Sorting at the Endoplasmic Reticulum Translocon of Proteins Destined for the Inner Nuclear Membrane |
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