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Adaptor proteins NUMB and NUMBL promote cell cycle withdrawal by targeting ERBB2 for degradation
Maretoshi Hirai, … , Ju Chen, Sylvia M. Evans
Maretoshi Hirai, … , Ju Chen, Sylvia M. Evans
Published January 9, 2017
Citation Information: J Clin Invest. 2017;127(2):569-582. https://doi.org/10.1172/JCI91081.
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Research Article Cardiology Development

Adaptor proteins NUMB and NUMBL promote cell cycle withdrawal by targeting ERBB2 for degradation

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Abstract

Failure of trabecular myocytes to undergo appropriate cell cycle withdrawal leads to ventricular noncompaction and heart failure. Signaling of growth factor receptor ERBB2 is critical for myocyte proliferation and trabeculation. However, the mechanisms underlying appropriate downregulation of trabecular ERBB2 signaling are little understood. Here, we have found that the endocytic adaptor proteins NUMB and NUMBL were required for downregulation of ERBB2 signaling in maturing trabeculae. Loss of NUMB and NUMBL resulted in a partial block of late endosome formation, resulting in sustained ERBB2 signaling and STAT5 activation. Unexpectedly, activated STAT5 overrode Hippo-mediated inhibition and drove YAP1 to the nucleus. Consequent aberrant cardiomyocyte proliferation resulted in ventricular noncompaction that was markedly rescued by heterozygous loss of function of either ERBB2 or YAP1. Further investigations revealed that NUMB and NUMBL interacted with small GTPase Rab7 to transition ERBB2 from early to late endosome for degradation. Our studies provide insight into mechanisms by which NUMB and NUMBL promote cardiomyocyte cell cycle withdrawal and highlight previously unsuspected connections between pathways that are important for cardiomyocyte cell cycle reentry, with relevance to ventricular noncompaction cardiomyopathy and regenerative medicine.

Authors

Maretoshi Hirai, Yoh Arita, C. Jane McGlade, Kuo-Fen Lee, Ju Chen, Sylvia M. Evans

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Figure 6

NUMB and NUMBL interact with Rab7, and YAP1 interacts with STAT5.

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NUMB and NUMBL interact with Rab7, and YAP1 interacts with STAT5.
(A) In...
(A) Interaction of FLAG-tagged NUMB with GST-tagged GDP- or GTP-bound Rabs. As expected, only the active GTPγS-bound form of Rab5a interacted with EEA1 (bottom panel), indicating that the addition of either GDP or GTPγS to Rab proteins was successful. NUMB interaction with Rab7a or Rab7b was readily detectable, whereas interactions between NUMB and Rab5a or Rab11a were detectable only upon prolonged exposure. Note preferential association of NUMB with the active GTPγS-bound form of Rab7a. (B) Live images of HeLa cells stably expressing EGFP-NUMB and mCherry-Rab7a with nuclear Hoechst 33342 staining. NUMB and Rab7a were strongly colocalized. Scale bar: 10 µm. (C) FLAG-tagged deletion constructs of Yap1 and Stat5. (D) Immunoprecipitation of FLAG-tagged Yap1 deletion constructs from cotransfected 293T cell extracts was followed by Western blot analysis with antibody to STAT5. Conversely, immunoprecipitation of FLAG-tagged Stat5 deletion constructs from cotransfected 293T cell extracts was followed by Western blot analysis with antibody to Myc. (E) Domains within YAP1 and STAT5 required for their interaction.
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