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. 2019 Dec 17;472(1):3–25. doi: 10.1007/s00424-019-02338-4

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — Interaction of RBP2 with Cav1.3 channels. RIMs and RBPs are multidomain proteins [41, 46]. All RIM isoforms (RIM1α and 1β; RIM2α, 2β, and 2γ; RIM3γ and RIM4γ) bind via their C₂B domain to the auxiliary β subunit of the Ca²⁺ channel complex. Disruption of the SH3 or GK domain in the β subunit prevents the interaction with RIM [28]. All three RBP isoforms contain three SH3 domains and two (RBP3) or three (RBP1 and 2) FN3 domains [41]. The second SH3 domain of RBP binds to the proline-rich region (PXXP) present only in RIMα or β isoforms, located between the two C₂ domains. The other SH3 domains, marked by “x,” in turn can interact with a proline-rich region (PXXP) localized in the full-length Cav1.3 C terminus [23]. Note that incorporation of alternative exons 42A and 43S leads to short C-terminal splice variants (Cav1.3_42A or Cav1.3_43S, respectively; C-terminal ends indicated by orange dots) lacking the PXXP interaction site. AID, α-interaction domain; FN3, fibronectin 3 domain; GK, guanylate-kinase like domain; PXXP, proline-rich region; SH3, SRC homology 3 domain; Zn²⁺, zinc finger domain. Note that RIM may also interact via its C₂B domain with the C terminus of Cav1.3, but the interaction site is unknown [49]