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Gravi-D peptide disrupts HDAC11 association with an AKAP to stimulate adipocyte thermogenic signaling
Emma L. Robinson, Charles A. Tharp, Rushita A. Bagchi, Timothy A. McKinsey
Emma L. Robinson, Charles A. Tharp, Rushita A. Bagchi, Timothy A. McKinsey
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Research Letter Cell biology

Gravi-D peptide disrupts HDAC11 association with an AKAP to stimulate adipocyte thermogenic signaling

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Abstract

Authors

Emma L. Robinson, Charles A. Tharp, Rushita A. Bagchi, Timothy A. McKinsey

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Figure 1

Gravi-D peptide stimulates adipocyte PKA signaling and UCP1 induction.

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Gravi-D peptide stimulates adipocyte PKA signaling and UCP1 induction.
(...
(A) Schematic representation of full-length and truncated forms of rat gravin-α. The 10–amino acid HDAC11 binding domain is indicated. (B) Coimmunoprecipitation of Myc-tagged HDAC11 with full-length (WT) and truncated forms of gravin-α in transfected HEK293 cells; gravin-α migrates as a monomer (M) and oligomer (O) in SDS-PAGE. (C) Schematic depiction of Gravi-D. (D) Schematic depiction of the lipid raft protein coimmunoprecipitation study. (E) Coimmunoprecipitation analysis of the indicated proteins. (F) 3T3-L1 adipocytes were treated with vehicle control or CL-316,243 (1 μM) for 30 minutes followed by scrambled peptide or Gravi-D for 1 additional hour, and harvested for immunoblotting. (G) Immunofluorescence images of 3T3-L1 adipocytes treated with vehicle (water), scrambled peptide (1 μM), or Gravi-D (1 μM) for 1 hour. Scale bars: 50 μm. (H) A model for Gravi-D–mediated induction of thermogenesis and lipolysis. For all blots, each lane represents protein from an independent plate of cells.

Copyright © 2026 American Society for Clinical Investigation
ISSN: 0021-9738 (print), 1558-8238 (online)

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