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Olaf Klingbeil , Damianos Skopelitis , Claudia Tonelli , Toyoki Yoshimoto , Aktan Alpsoy , Maria C. Panepinto , Francesca Minicozzi , Joseph R. Merrill , Amanda M. Cafiero , Disha Aggarwal , Suzanne Russo , Taehoon Ha , Osama E. Demerdash , Tse-Luen Wee , David L. Spector , Scott K. Lyons , David A. Tuveson , Paolo Cifani , Christopher R. Vakoc ·

YOU? · · 2024 · Open Access · · DOI: https://doi.org/10.1158/2159-8290.27938735

A-E, Western blot analysis of MARK2 specific substrates phosphorylation. Labeling as described in Fig 3D. Data are representative of two independent experiments. F, Lolli-pop illustration of MARK2-dependent phosphorylation sites on MST1/2 and MAP4K1-4,6,7 identified using mass spectrometry-based phosphoproteomics. SARAH= Sav/Rassf/Hpo domain, CNH= Citron homology domain. G, IP–western blot analysis evaluating the phosphorylation p-LATS2 (T1041) in the presence or absence of MARK2 or MARK3 following NF2 overexpression in HEK-293T cells. Data are representative of two independent experiments. H, IP–western blot analysis evaluating the phosphorylation p-LATS2 (T1041) after NF2 mutant overexpression in HEK-293T cells. Data are representative of two independent experiments. I, IP–western blot analysis evaluating p-LATS1 (T1079) in the presence of NF2 together with MARK2 overexpression in HEK-293T cells. Data are representative of two independent experiments. J, IP–western blot analysis evaluating the interaction of NF2 and MAP4K4,6,7 in the presence or absence of MARK2 overexpression in HEK-293T cells. Data are representative of two independent experiments. K, IP–western blot analysis evaluating the phosphorylation p-LATS1 (T1079) following indicated gene overexpression in HEK-293T cells. L, IP–western blot analysis evaluating the phosphorylation p-LATS1 (T1079) following indicated gene overexpression in HEK-293T cells. Data are representative of two independent experiments. M, IP–western blot analysis evaluating p-LATS1 (T1079) in the presence of MAP4K4 or MAP4K6 together with MARK2,3, kinase-dead MARK2K82H or empty vector control overexpression in HEK-293T cells. Data are representative of two independent experiments. N, O, IP–western blot analysis evaluating p-LATS1 (T1079) in the presence of MAP4K4 or MST1 mutants. Data are representative of two independent experiments. P, Coomassie stain of recombinant proteins used in in vitro kinase assays (Fig.4D, 3E), purified from bacteria (GST-YAP, GST-TAZ) and insect cells. Q, R, In vitro kinase assay using recombinant full-length GST-YAP (P) or synthetically synthesized S128-phosphorylated peptide (Q) together with recombinant LATS2 followed by Mass spectrometry analysis of double phosphorylated YAP peptides. F was created with BioRender.com.

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HEK 293 cells Western blot Phosphorylation Molecular biology Blot Kinase Chemistry Biology Cell biology Gene Biochemistry

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Type: preprint
Language: en
Landing Page: https://doi.org/10.1158/2159-8290.27938735
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Title: Supplementary Figure S6 from MARK2/MARK3 Kinases Are Catalytic Codependencies of YAP/TAZ in Human Cancer

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Publication year: 2024

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Authors: Olaf Klingbeil, Damianos Skopelitis, Claudia Tonelli, Toyoki Yoshimoto, Aktan Alpsoy, Maria C. Panepinto, Francesca Minicozzi, Joseph R. Merrill, Amanda M. Cafiero, Disha Aggarwal, Suzanne Russo, Taehoon Ha, Osama E. Demerdash, Tse-Luen Wee, David L. Spector, Scott K. Lyons, David A. Tuveson, Paolo Cifani, Christopher R. Vakoc

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Concepts: HEK 293 cells, Western blot, Phosphorylation, Molecular biology, Blot, Kinase, Chemistry, Biology, Cell biology, Gene, Biochemistry

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abstract_inverted_index.purified	264
abstract_inverted_index.specific	6
abstract_inverted_index.together	111, 207, 289
abstract_inverted_index.(GST-YAP,	267
abstract_inverted_index.Coomassie	251
abstract_inverted_index.Lolli-pop	23
abstract_inverted_index.MARK2K82H	211
abstract_inverted_index.described	11
abstract_inverted_index.following	63, 163, 179
abstract_inverted_index.indicated	164, 180
abstract_inverted_index.peptides.	302
abstract_inverted_index.MAP4K4,6,7	135
abstract_inverted_index.evaluating	49, 80, 103, 129, 158, 174, 197, 232
abstract_inverted_index.identified	33
abstract_inverted_index.substrates	7
abstract_inverted_index.full-length	280
abstract_inverted_index.independent	20, 74, 97, 123, 152, 191, 225, 248
abstract_inverted_index.interaction	131
abstract_inverted_index.kinase-dead	210
abstract_inverted_index.recombinant	254, 279, 291
abstract_inverted_index.synthesized	285
abstract_inverted_index.IP–western	46, 77, 100, 126, 155, 171, 194, 229
abstract_inverted_index.MAP4K1-4,6,7	32
abstract_inverted_index.experiments.	21, 75, 98, 124, 153, 192, 226, 249
abstract_inverted_index.illustration	24
abstract_inverted_index.spectrometry	296
abstract_inverted_index.<p>A-E,	0
abstract_inverted_index.Sav/Rassf/Hpo	39
abstract_inverted_index.synthetically	284
abstract_inverted_index.overexpression	65, 88, 114, 143, 166, 182, 216
abstract_inverted_index.phosphorylated	300
abstract_inverted_index.representative	17, 71, 94, 120, 149, 188, 222, 245
abstract_inverted_index.MARK2-dependent	26
abstract_inverted_index.phosphorylation	27, 51, 82, 160, 176
abstract_inverted_index.phosphorylation.	8
abstract_inverted_index.phosphoproteomics.	37
abstract_inverted_index.spectrometry-based	36
abstract_inverted_index.S128-phosphorylated	286
abstract_inverted_index.BioRender.com.</p>	307
cited_by_percentile_year
countries_distinct_count	0
institutions_distinct_count	19
citation_normalized_percentile.value	0.28384968
citation_normalized_percentile.is_in_top_1_percent	False
citation_normalized_percentile.is_in_top_10_percent	False