| Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane. | Distinct domains in Ndc1 mediate its interaction with the Nup84 complex and the nuclear membrane.
Amm I, Weberruss M, Hellwig A, Schwarz J, Tatarek-Nossol M, Lüchtenborg C, Kallas M, Brügger B, Hurt E, Antonin W., Free PMC Article | 05/10/2023 |
| A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription. | A nuclear pore sub-complex restricts the propagation of Ty retrotransposons by limiting their transcription.
Bonnet A, Chaput C, Palmic N, Palancade B, Lesage P., Free PMC Article | 12/4/2021 |
| A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure. | A nanobody suite for yeast scaffold nucleoporins provides details of the nuclear pore complex structure.
Nordeen SA, Andersen KR, Knockenhauer KE, Ingram JR, Ploegh HL, Schwartz TU., Free PMC Article | 12/19/2020 |
| The Nup84 complex coordinates the DNA damage response to insure genome integrity. | The Nup84 complex coordinates the DNA damage response to warrant genome integrity.
Gaillard H, Santos-Pereira JM, Aguilera A., Free PMC Article | 11/30/2019 |
| The kinesin-14 motor protein complex (Cik1-Kar3) cooperates with chromatin remodellers to mediate interactions between subtelomeric double-strand breaks and the Nup84 nuclear pore complex to ensure cell survival via break-induced replication. | Perinuclear tethers license telomeric DSBs for a broad kinesin- and NPC-dependent DNA repair process.
Chung DK, Chan JN, Strecker J, Zhang W, Ebrahimi-Ardebili S, Lu T, Abraham KJ, Durocher D, Mekhail K. | 05/14/2016 |
| This study provides evidence for a new role of the Nup84 complex and a number of mRNA processing factors in transcription elongation that supports a connection of pre-mRNA processing and nuclear export with transcription elongation. | A novel assay identifies transcript elongation roles for the Nup84 complex and RNA processing factors.
Tous C, Rondón AG, García-Rubio M, González-Aguilera C, Luna R, Aguilera A., Free PMC Article | 07/30/2011 |
| crystal structure of the heterotrimeric Sec13 x Nup145C x Nup84 complex, centerpiece of the heptamer, at 3.2-A resolution. Nup84 forms a U-shaped alpha-helical solenoid domain, topologically similar to two other members of the heptamer, Nup145C and Nup85 | Structure of a trimeric nucleoporin complex reveals alternate oligomerization states.
Nagy V, Hsia KC, Debler EW, Kampmann M, Davenport AM, Blobel G, Hoelz A., Free PMC Article | 01/21/2010 |
| The heterotypic ACE1 interaction of Nup84 and Nup145C is analogous to the homotypic ACE1 interaction of Sec31 that forms COPII lattice edge elements and is inconsistent with the alternative 'fence-like' NPC model. | Molecular architecture of the Nup84-Nup145C-Sec13 edge element in the nuclear pore complex lattice.
Brohawn SG, Schwartz TU., Free PMC Article | 01/21/2010 |
| As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure. | Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex.
Seo HS, Ma Y, Debler EW, Wacker D, Kutik S, Blobel G, Hoelz A., Free PMC Article | 01/21/2010 |
| Results describe the three-dimensional structure of a putative membrane-coating subcomplex of the nuclear pore complex, the heptameric Nup84 complex. | Three-dimensional structure and flexibility of a membrane-coating module of the nuclear pore complex.
Kampmann M, Blobel G., Free PMC Article | 01/21/2010 |
| Data show that Rap1/Gcr1/Gcr2 transcriptional activation in yeast cells occurs through a large anchored protein platform, the Nup84 nuclear pore subcomplex. | Reverse recruitment: the Nup84 nuclear pore subcomplex mediates Rap1/Gcr1/Gcr2 transcriptional activation.
Menon BB, Sarma NJ, Pasula S, Deminoff SJ, Willis KA, Barbara KE, Andrews B, Santangelo GM., Free PMC Article | 01/21/2010 |