Members in Tourism Settings – their motivations, behaviours and roles

Membership programs are widely-used marketing tools. Many customers belong to a number of different membership programs across a variety of organizations and contexts. Memberships are based on the idea of mutual benefits of a relationship. Memberships in general offer tangible and intangible benefits such as free admission, discounts, special offers or access to special services, and a sense of belonging and identity. General organizational benefits of memberships besides customers are funding, fee revenue, legitimacy, and various kinds of member support. Memberships are used as competitive relationship marketing tools to retain customers, build relationships and encourage member participation. Many memberships have developed from merely being reward programs into an attempt to create emotional bonds based on calculative and affective commitment. Research into memberships is an emergent multidisciplinary field of interest for practitioners and scholars representing different disciplines. This thesis is delimited to study members and memberships at nonprofit organizations within tourism settings from a relationship marketing perspective. The aim is to get insight into why individuals choose to become members, why they stay on as members, and how members interact and use their memberships. The overall objective is therefore to explore motivations related to memberships and how this is reflected in different member behaviours and member roles within tourism settings. Throughout this thesis a mixed-method research approach was applied combining qualitative and quantitative research to explore the membership phenomenon. This thesis is comprised of four studies based on data from an explorative pre-study (12 respondents), a questionnaire survey (755 respondents), and a Nordic cross-case study (37 respondents). Findings showed member motivations, behaviours and roles within the tourism system. Member motivations were identified as altruistic (doing good for others), self-interest (doing good for yourself) and social (doing good with others). Findings further showed member interactions with other members (M2M), customers/visitors (M2C) and supported organizations (M2B). Member behaviours found were: returning (retention); supporting, visiting, using member information (participation); marketing, spreading WOM and recruiting new members; and volunteering (co-creation). Furthermore, significant relations were found between motivational dimensions, behaviours and member demographics (age, gender, and distance). Members performed multiple overlapping roles from being supporters and visitors to front-line co-creators

Protonation and Hydrogen Bonding of Ca2+ Site Residues in the E2P Phosphoenzyme Intermediate of Sarcoplasmic Reticulum Ca2+-ATPase Studied by a Combination of Infrared Spectroscopy and Electrostatic Calculations

Protonation of the Ca2+ ligands of the SR Ca2+-ATPase (SERCA1a) was studied by a combination of rapid scan FTIR spectroscopy and electrostatic calculations. With FTIR spectroscopy, we investigated the pH dependence of C=O bands of the Ca2+-free phosphoenzyme (E2P) and obtained direct experimental evidence for the protonation of carboxyl groups upon Ca2+ release. At least three of the infrared signals from protonated carboxyl groups of E2P are pH dependent with pKa values near 8.3: a band at 1758 cm−1 characteristic of nonhydrogen-bonded carbonyl groups, a shoulder at 1720 cm−1, and part of a band at 1710 cm−1, both characteristic of hydrogen-bonded carbonyl groups. The bands are thus assigned to H+ binding residues, some of which are involved in H+ countertransport. At pH 9, bands at 1743 and 1710 cm−1 remain which we do not attribute to Ca2+/H+ exchange. We also obtained evidence for a pH-dependent conformational change in β-sheet or turn structures of the ATPase. With MCCE on the E2P analog E2(\documentclass[10pt]{article} \usepackage{amsmath} \usepackage{wasysym} \usepackage{amsfonts} \usepackage{amssymb} \usepackage{amsbsy} \usepackage{mathrsfs} \usepackage{pmc} \usepackage[Euler]{upgreek} \pagestyle{empty} \oddsidemargin -1.0in \begin{document} \begin{equation*}{\mathrm{TG}}+{\mathrm{MgF}}_{4}^{2-}\end{equation*}\end{document}), we assigned infrared bands to specific residues and analyzed whether or not the carbonyl groups of the acidic Ca2+ ligands are hydrogen bonded. The carbonyl groups of Glu771, Asp800, and Glu908 were found to be hydrogen bonded and will thus contribute to the lower wave number bands. The carbonyl group of some side-chain conformations of Asp800 is left without a hydrogen-bonding partner; they will therefore contribute to the higher wave number band

ATF4 Degradation Relies on a Phosphorylation-Dependent Interaction with the SCF(βTrCP) Ubiquitin Ligase

The ubiquitin-proteasome pathway regulates gene expression through protein degradation. Here we show that the F-box protein βTrCP, the receptor component of the SCF E3 ubiquitin ligase responsible for IκBα and β-catenin degradation, is colocalized in the nucleus with ATF4, a member of the ATF-CREB bZIP family of transcription factors, and controls its stability. Association between the two proteins depends on ATF4 phosphorylation and on ATF4 serine residue 219 present in the context of DSGXXXS, which is similar but not identical to the motif found in other substrates of βTrCP. ATF4 ubiquitination in HeLa cells is enhanced in the presence of βTrCP. The F-box-deleted βTrCP protein behaves as a negative transdominant mutant that inhibits ATF4 ubiquitination and degradation and, subsequently, enhances its activity in cyclic AMP-mediated transcription. ATF4 represents a novel substrate for the SCF(βTrCP) complex, which is the first mammalian E3 ubiquitin ligase identified so far for the control of the degradation of a bZIP transcription factor