High resolution angle-resolved photoemission spectroscopy data along the (0,0)-(π,π) nodal direction with significantly improved statistics reveal fine structure in the electron self-energy of the underdoped (La2−xSrx)CuO4 samples in the normal state. Fine structure at energies of (40∼46) meV and (58∼63)meV, and possible fine structure at energies of (23∼29)meV and (75∼85)meV, have been identified. These observations indicate that, in LSCO, more than one bosonic modes are involved in the coupling with electrons.PACS numbers: 74.25.Jb,71.18.+y,74.72.Dn, The recent observation of the electron self-energy renormalization effect in the form of a "kink" in the dispersion has generated considerable interest because it reveals a coupling of the electrons with a collective boson mode of the cuprate superconductors [1]. However, the nature of the bosons involved remains controversial mainly because the previous experiments can only be used to determine an approximate energy of the mode and this energy is close to both the optical phonon [2,3] and the spin resonance [4]. Determining the nature of the mode(s) that couple to the electrons is likely important in understanding the pairing mechanism of superconductivity.In conventional superconductors, identification of the fine structure for the phonon anomalies in the tunnelling spectra has played a decisive role in reaching a consensus on the nature of the bosons involved [5]. The fine structure provides fingerprints for much more stringent comparison with known boson spectra. So far, such fine structure has not been detected in the angleresolved photoemission spectroscopy (ARPES) data. In this Letter we present significantly improved high resolution ARPES data of (La 2−x Sr x )CuO 4 (LSCO) that, for the first time, reveal fine structure in the electron selfenergy, demonstrating the involvement of multiple boson modes in the coupling with electrons.The photoemission measurements were carried out on beamline 10.0.1 at the ALS, using Scienta 2002 and R4000 electron energy analyzers. As high energy resolution and high data statistics are crucial to identify fine structure in the electron self-energy, the experimental conditions were set to compromise between these two conflicting requirements. The measurement is particularly challenging for LSCO system because of the necessity to use a relatively high photon energy (55eV). Different energy resolution between 12 and 20 meV was used for various measurements on different samples, and the angular resolution is 0.3 degree. An example of the high quality of the raw data is shown in Figs. 1a and 1b. Due to space charge problem, the Fermi level calibration has a ±5 meV uncertainty. We mainly present our data on the heavily underdoped LSCO x=0.03 (nonsuperconducting), LSCO x=0.063 (T c =12 K) and LSCO x=0.07 (T c =14 K) samples. These heavily underdoped LSCO samples are best candidates because they exhibit a stronger band renormalization effect above T c [3]; a relatively large magnitude of the real self-energy makes the identification...

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Secretory pore-forming proteins (PFPs) have been identified in organisms from all kingdoms of life. Our studies with the toad species Bombina maxima found an interaction network among aerolysin family PFPs (af-PFPs) and trefoil factors (TFFs). As a toad af-PFP, BmALP1 can be reversibly regulated between active and inactive forms, with its paralog BmALP3 acting as a negative regulator. BmALP1 interacts with BmTFF3 to form a cellular active complex called βγ-CAT. This PFP complex is characterized by acting on endocytic pathways and forming pores on endolysosomes, including stimulating cell macropinocytosis. In addition, cell exocytosis can be induced and/or modulated in the presence of βγ-CAT. Depending on cell contexts and surroundings, these effects can facilitate the toad in material uptake and vesicular transport, while maintaining mucosal barrier function as well as immune defense. Based on experimental evidence, we hereby propose a secretory endolysosome channel (SELC) pathway conducted by a secreted PFP in cell endocytic and exocytic systems, with βγ-CAT being the first example of a SELC protein. With essential roles in cell interactions and environmental adaptations, the proposed SELC protein pathway should be conserved in other living organisms.