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Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia

Cobll1 affects blast crisis (BC) progression and tyrosine kinase inhibitor (TKI) resistance in chronic myeloid leukemia (CML). PACSIN2, a novel Cobll1 binding protein, activates TKI‐induced apoptosis in K562 cells, and this activation is suppressed by Cobll1 through the interaction between PACSIN2 a...

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Autores principales: Park, Kibeom, Yoo, Hee‐Seop, Oh, Chang‐Kyu, Lee, Joo Rak, Chung, Hee Jin, Kim, Ha‐Neul, Kim, Soo‐Hyun, Kee, Kyung‐Mi, Kim, Tong Yoon, Kim, Myungshin, Kim, Byung‐Gyu, Ra, Jae Sun, Myung, Kyungjae, Kim, Hongtae, Han, Seung Hun, Seo, Min‐Duk, Lee, Yoonsung, Kim, Dong‐Wook
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9636508/
https://www.ncbi.nlm.nih.gov/pubmed/35352878
http://dx.doi.org/10.1002/cam4.4727
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author Park, Kibeom
Yoo, Hee‐Seop
Oh, Chang‐Kyu
Lee, Joo Rak
Chung, Hee Jin
Kim, Ha‐Neul
Kim, Soo‐Hyun
Kee, Kyung‐Mi
Kim, Tong Yoon
Kim, Myungshin
Kim, Byung‐Gyu
Ra, Jae Sun
Myung, Kyungjae
Kim, Hongtae
Han, Seung Hun
Seo, Min‐Duk
Lee, Yoonsung
Kim, Dong‐Wook
author_facet Park, Kibeom
Yoo, Hee‐Seop
Oh, Chang‐Kyu
Lee, Joo Rak
Chung, Hee Jin
Kim, Ha‐Neul
Kim, Soo‐Hyun
Kee, Kyung‐Mi
Kim, Tong Yoon
Kim, Myungshin
Kim, Byung‐Gyu
Ra, Jae Sun
Myung, Kyungjae
Kim, Hongtae
Han, Seung Hun
Seo, Min‐Duk
Lee, Yoonsung
Kim, Dong‐Wook
author_sort Park, Kibeom
collection PubMed
description Cobll1 affects blast crisis (BC) progression and tyrosine kinase inhibitor (TKI) resistance in chronic myeloid leukemia (CML). PACSIN2, a novel Cobll1 binding protein, activates TKI‐induced apoptosis in K562 cells, and this activation is suppressed by Cobll1 through the interaction between PACSIN2 and Cobll1. PACSIN2 also binds and inhibits SH3BP1 which activates the downstream Rac1 pathway and induces TKI resistance. PACSIN2 competitively interacts with Cobll1 or SH3BP1 with a higher affinity for Cobll1. Cobll1 preferentially binds to PACSIN2, releasing SH3BP1 to promote the SH3BP1/Rac1 pathway and suppress TKI‐mediated apoptosis and eventually leading to TKI resistance. Similar interactions among Cobll1, PACSIN2, and SH3BP1 control hematopoiesis during vertebrate embryogenesis. Clinical analysis showed that most patients with CML have Cobll1 and SH3BP1 expression at the BC phase and BC patients with Cobll1 and SH3BP1 expression showed severe progression with a higher blast percentage than those without any Cobll1, PACSIN2, or SH3BP1 expression. Our study details the molecular mechanism of the Cobll1/PACSIN2/SH3BP1 pathway in regulating drug resistance and BC progression in CML.
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spelling pubmed-96365082022-11-07 Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia Park, Kibeom Yoo, Hee‐Seop Oh, Chang‐Kyu Lee, Joo Rak Chung, Hee Jin Kim, Ha‐Neul Kim, Soo‐Hyun Kee, Kyung‐Mi Kim, Tong Yoon Kim, Myungshin Kim, Byung‐Gyu Ra, Jae Sun Myung, Kyungjae Kim, Hongtae Han, Seung Hun Seo, Min‐Duk Lee, Yoonsung Kim, Dong‐Wook Cancer Med RESEARCH ARTICLES Cobll1 affects blast crisis (BC) progression and tyrosine kinase inhibitor (TKI) resistance in chronic myeloid leukemia (CML). PACSIN2, a novel Cobll1 binding protein, activates TKI‐induced apoptosis in K562 cells, and this activation is suppressed by Cobll1 through the interaction between PACSIN2 and Cobll1. PACSIN2 also binds and inhibits SH3BP1 which activates the downstream Rac1 pathway and induces TKI resistance. PACSIN2 competitively interacts with Cobll1 or SH3BP1 with a higher affinity for Cobll1. Cobll1 preferentially binds to PACSIN2, releasing SH3BP1 to promote the SH3BP1/Rac1 pathway and suppress TKI‐mediated apoptosis and eventually leading to TKI resistance. Similar interactions among Cobll1, PACSIN2, and SH3BP1 control hematopoiesis during vertebrate embryogenesis. Clinical analysis showed that most patients with CML have Cobll1 and SH3BP1 expression at the BC phase and BC patients with Cobll1 and SH3BP1 expression showed severe progression with a higher blast percentage than those without any Cobll1, PACSIN2, or SH3BP1 expression. Our study details the molecular mechanism of the Cobll1/PACSIN2/SH3BP1 pathway in regulating drug resistance and BC progression in CML. John Wiley and Sons Inc. 2022-03-30 /pmc/articles/PMC9636508/ /pubmed/35352878 http://dx.doi.org/10.1002/cam4.4727 Text en © 2022 The Authors. Cancer Medicine published by John Wiley & Sons Ltd. https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle RESEARCH ARTICLES
Park, Kibeom
Yoo, Hee‐Seop
Oh, Chang‐Kyu
Lee, Joo Rak
Chung, Hee Jin
Kim, Ha‐Neul
Kim, Soo‐Hyun
Kee, Kyung‐Mi
Kim, Tong Yoon
Kim, Myungshin
Kim, Byung‐Gyu
Ra, Jae Sun
Myung, Kyungjae
Kim, Hongtae
Han, Seung Hun
Seo, Min‐Duk
Lee, Yoonsung
Kim, Dong‐Wook
Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia
title Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia
title_full Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia
title_fullStr Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia
title_full_unstemmed Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia
title_short Reciprocal interactions among Cobll1, PACSIN2, and SH3BP1 regulate drug resistance in chronic myeloid leukemia
title_sort reciprocal interactions among cobll1, pacsin2, and sh3bp1 regulate drug resistance in chronic myeloid leukemia
topic RESEARCH ARTICLES
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9636508/
https://www.ncbi.nlm.nih.gov/pubmed/35352878
http://dx.doi.org/10.1002/cam4.4727
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