The calmodulin‐binding tetraleucine motif of KCNE4 is responsible for association with Kv1.3

• DOI: 10.1096/fj.201801164rr
• Publication Date: 2019-04-10T18:45:02Z
• Authors: Laura Solé; Sara R. Roig; Daniel Sastre; Albert Vallejo-Gr...; Antonio Serrano-A...; Antonio Ferrer-Mo...; Gregorio Fernánde...; Michael M. Tamkun; Antonio Felipe
• Keywords: ER retention; Motif (music); Subfamily

The voltage-dependent potassium (Kv) channel Kv1.3 regulates leukocyte proliferation, activation, and apoptosis, altered expression of this is linked to autoimmune diseases. Thus, the fine-tuning function crucial for immune system response. accessory protein, voltage-gated subfamily E (KCNE) subunit 4, acts as a dominant negative regulatory both enhance inactivation induce intracellular retention Kv1.3. Mutations in KCNE4 also cause dysfunction. Although formation Kv1.3-KCNE4 complexes has profound consequences physiology, molecular determinants involved association are unknown. We now show that associates with via tetraleucine motif situated within carboxy-terminal domain protein. This would an interaction platform, which Ca2+/calmodulin compete interaction. Finally, we propose structural model complex. Our experimental data silico structure suggest hides forward-trafficking addition adding strong endoplasmic reticulum signature oligomeric composition channelosome fine-tunes precise balance between anterograde elements control cell surface physiology.—Sole, L., Roig, S. R., Sastre, D., Vallejo-Gracia, A., Serrano-Albarrás, Ferrer-Montiel, Fernández-Ballester, G., Tamkun, M. M., Felipe, A. calmodulin-binding responsible FASEB J. 33, 8263–8279 (2019). www.fasebj.org