An NH2-terminal domain of PALB2, distinct from the BRCA2-interacting domain of PALB2, mediates interaction with BRCA1 and assembly of PALB2 nuclear foci.

Slides:

Advertisements

Similar presentations

Interaction of Stau1 with ribosomal protein P0 (A) Schematic representation of Stau1, showing its dRBDs I–IV (boxes) and PP1 interaction domain (circle),

Advertisements

Constitutive NF-κB activation by the t(11;18)(q21;q21) product in MALT lymphoma is linked to deregulated ubiquitin ligase activity Honglin Zhou, Ming-Qing.

Implications of somatic mutations in the AML1 gene in radiation-associated and therapy-related myelodysplastic syndrome/acute myeloid leukemia by Hironori.

Patient-derived C-terminal mutation of FANCI causes protein mislocalization and reveals putative EDGE motif function in DNA repair by Luca Colnaghi, Mathew.

Pirh2 promotes p73 ubiquitination in vivo.

Phosphorylation of NF-κB p65 by PKA Stimulates Transcriptional Activity by Promoting a Novel Bivalent Interaction with the Coactivator CBP/p300 Haihong.

Volume 134, Issue 2, Pages (July 2008)

Volume 15, Issue 22, Pages (November 2005)

Volume 45, Issue 5, Pages (March 2012)

Claudia D. Andl, John R. Stanley Journal of Investigative Dermatology

Coiled Coils Direct Assembly of a Cold-Activated TRP Channel

Volume 45, Issue 1, Pages (January 2012)

SYCE2 directly binds to the chromoshadow domain of HP1α.

Interfering with HMGA2 expression blocks transformation in metastatic lung cancer cells. Interfering with HMGA2 expression blocks transformation in metastatic.

Volume 11, Issue 21, Pages (October 2001)

Volume 12, Issue 5, Pages (November 2003)

Volume 9, Issue 3, Pages (March 2009)

ER Stress Regulation of ATF6 Localization by Dissociation of BiP/GRP78 Binding and Unmasking of Golgi Localization Signals Jingshi Shen, Xi Chen, Linda.

Localization of the Iff8 extended protein.

p38 MAPK activation is required for phosphorylation of Akt at Ser473.

HOXB7 interacts with ERα and enhances expression of ER target genes.

Volume 17, Issue 8, Pages (April 2007)

Volume 3, Issue 6, Pages (December 2002)

Volume 15, Issue 10, Pages (June 2016)

Proteomics analysis of NaPi-IIa C terminus binding to PDZ proteins.

Volume 43, Issue 4, Pages (October 2015)

Eaf3 Chromodomain Interaction with Methylated H3-K36 Links Histone Deacetylation to Pol II Elongation Amita A. Joshi, Kevin Struhl Molecular Cell Volume.

Effect of expression of constitutively active CAMKK2 on AMPK activation and the cell cycle in G361 cells. Effect of expression of constitutively active.

Binding of recombinant laminin-111, laminin-511, and their EQ mutants to integrins. Binding of recombinant laminin-111, laminin-511, and their EQ mutants.

Shrestha Ghosh, Baohua Liu, Yi Wang, Quan Hao, Zhongjun Zhou

IgG Autoantibodies from Bullous Pemphigoid Patients Recognize Multiple Antigenic Reactive Sites Located Predominantly Within the B and C Subdomains of.

Abraxas binds to BRCT–PALB2(L21P) and is involved in the recruitment of this fusion protein or of endogenous PALB2 to sites of DNA damage. Abraxas binds.

Fusion of PALB2 to the BRCT repeats of BRCA1 mediates the assembly of DNA damage foci by PALB2 and RAD51 in BRCA1-deficient cells. Fusion of PALB2 to the.

Fusion of PALB2(L21P) to the BRCT repeats of BRCA1 mediates the assembly of DNA damage foci by PALB2 and RAD51 in PALB2-deficient cells. Fusion of PALB2(L21P)

Figure 4 DNM1 mutations affect protein levels and self-dimerization (A) HeLa cells were transfected with green fluorescent protein (GFP)-tagged mutant.

14-3-3γ phosphorylated at S59 by Lats2 in response to UV damage.

PALB2 is recruited by a pathway that mediates and recognizes protein ubiquitination at sites of DNA damage. PALB2 is recruited by a pathway that mediates.

Segments R1, R3, R6 and R7, and GTPase activity of Mfn2ΔTM are necessary for mitochondrial fragmentation in COS7 cells. Segments R1, R3, R6 and R7, and.

eNOS regulated IR-induced NO generation and EGFR signal activation.

Volume 43, Issue 5, Pages (September 2011)

Enhancement of BLM-DNA2-Mediated Long-Range DNA End Resection by CtIP

Figure 2 Antibodies to MOG detected with anti-human IgG (H + L) as the secondary antibody(A) Schematic of the human MOG proteins tested. Antibodies to.

co-IP of LEDGF/p75 and MeCP2.

In vitro interaction domain mapping of pVHL and AUF1.

Constitutive NF-κB activation by the t(11;18)(q21;q21) product in MALT lymphoma is linked to deregulated ubiquitin ligase activity Honglin Zhou, Ming-Qing.

CDCP1 colocalizes and interacts with MT1-MMP.

Mapping the Pirh2 and p73 interaction sites.

NF-kB binds to the NF-κB binding site immediately adjacent to the AT-rich regulatory region. NF-kB binds to the NF-κB binding site immediately adjacent.

Clathrin-dependent, constitutive endocytosis of DR4 and DR5 in TRAIL-resistant cells. Clathrin-dependent, constitutive endocytosis of DR4 and DR5 in TRAIL-resistant.

Proposed model for the role of PALB2 in linking BRCA1 with BRCA2 and RAD51 in a pathway of HR. We propose that BRCA1 binds to the NH2 terminus of PALB2.

by Kevin J. Paavola, Harwin Sidik, J

PHF10 acts as a transcriptional repressor.

PTB-independent ShcA pools employ distinct domains to hyperactivate mTOR and Src signaling. PTB-independent ShcA pools employ distinct domains to hyperactivate.

PTB-independent ShcA pools require a functional SH2 domain, but not the tyrosine phosphorylation sites to promote mammary tumorigenesis. PTB-independent.

A, structure of the deduced polypeptides coded by MAGE-E1 mRNAs.

Volume 2, Issue 3, Pages (September 1998)

Structures of wild-type and mutated recombinant CDX2.

N1 decoys differently inhibit ligand-induced NOTCH signaling.

SAHA blocks IR-induced increase of RAD51 protein in MM cells.

Volume 13, Issue 1, Pages (October 2015)

Fig. 6 The C9ORF72/SMCR8 complex regulates ULK1.

The interaction of PALB2 with BRCA1 is required for the assembly of PALB2, BRCA2, and RAD51 nuclear foci. The interaction of PALB2 with BRCA1 is required.

Interaction of NHEJ and HR pathways in PCO cultures.

FIH hydroxylates G9a and GLP at asparagine residues.

Association of TCTP with Pim-3 in human pancreatic cancer cell lines.

The LIN-2/LIN-7/LIN-10 Complex Mediates Basolateral Membrane Localization of the C. elegans EGF Receptor LET-23 in Vulval Epithelial Cells Susan M Kaech,

The interaction between PARsylated BRCA1 and RAP80 is required for maintaining BRCA1–RAP80–PARP1 complex integrity after DNA damage and normal HRR regulation.

Structural Basis of SOSS1 Complex Assembly and Recognition of ssDNA

Stable Cx43 expression in infected Cx43−/− cells and phosphorylation of Cx43. Stable Cx43 expression in infected Cx43−/− cells and phosphorylation of Cx43.

Inhibition of HDACs disrupts DNMT1 association with Hsp90.

Presentation transcript:

An NH2-terminal domain of PALB2, distinct from the BRCA2-interacting domain of PALB2, mediates interaction with BRCA1 and assembly of PALB2 nuclear foci. An NH2-terminal domain of PALB2, distinct from the BRCA2-interacting domain of PALB2, mediates interaction with BRCA1 and assembly of PALB2 nuclear foci. A. Diagram of sets of PALB2 mutants used to examine the interaction of PALB2 with BRCA1. These included large NH2- or COOH-terminal truncations (i), a series of smaller NH2-terminal truncations (ii), and two different point mutants (*) within the NH2-terminal coiled-coil domain of PALB2 (iii). Each PALB2 construct contained a Flag-HA epitope tag. In the case of NH2-terminal deletion mutants, the epitope tags were at the COOH terminus of the protein. All other constructs contained NH2-terminal epitope tags. FL, PALB2-full-length. B. Immunoprecipitation with anti-Flag antibodies was done for each experimental set. Antibodies against BRCA1, and BRCA2 or RAD51 in i, were used to determine whether the protein was present in immunoprecipitates. C. Diagram of amino acids 1 to 70 of PALB2. The predicted coiled-coil domain is underlined (amino acids 9-44); *, point mutants that were tested (L21P and L24P). D. Examples of PALB2 foci assembled by wild-type protein, PALB2/1-550, or PALB2-L21P following expression in 293T cells. Assembly of expressed PALB2 and its mutants, all of which contained an HA-Flag epitope tag, was detected with anti-HA antibodies. E. Quantification of the assembly of PALB2 foci, detected with anti-HA antibodies against the epitope tag for each set of mutants. Values for wild-type PALB2 and PALB2Δ1-70 are repeated in each data set for the purpose of comparison. Cells were fixed at 16 h following treatment with 15 Gy IR. Average values ± SD were determined from three independent counts of 150 or more cells each. Fan Zhang et al. Mol Cancer Res 2009;7:1110-1118 ©2009 by American Association for Cancer Research