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The protein encoded by SYTL2 is a synaptotagmin-like protein (SLP) that belongs to a C2 domain-containing protein family. Additionally we are shipping SYTL2 Antibodies (21) and SYTL2 Kits (4) and many more products for this protein.
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Our findings indicate that Slp2-a controls renal cell size through regulation of Rap (show LRPAP1 Proteins)-ezrin (show EZR Proteins) signaling independently of Rab27 (show RAB27A Proteins).
Slp2-a is required for targeting of the signaling molecule podocalyxin (show PODXL Proteins) to the apical membrane in a Rab27A (show RAB27A Proteins)-dependent manner.
Calmodulin (show Calm2 Proteins) suppresses synaptotagmin-2 (show SYT2 Proteins) transcription in cortical neurons
Loss of Slp2-a protein also induced a change in melanocyte morphology, from their normal elongated shape to a more rounded shape, which depended on the phospholipid-binding activity of Slp2-a
Slp2-a is part of the mucin (show SLC13A2 Proteins) secretory machinery in surface mucous cells of mouse stomach
These results suggest that both Slp1 and Slp2-a may form part of a docking complex, capturing secretory lysosomes at the immunological synapse.
The structural characterization of the Rab27a (show RAB27A Proteins)-exophilin4/Slp2-a complex will clarify Rab27 (show RAB27A Proteins) recognition by its effectors prior to vesicle tethering and docking.
The observed structural complementation between the interacting surfaces of Rab27a (show RAB27A Proteins) and Exophilin4 sheds light on the disparities among the Rab27 (show RAB27A Proteins) effectors and outlines a general mechanism for their recruitment.[exophilin4]
Syt2 (show SYT2 Proteins) can serve as an exocytic sensor for diverse Ca(2 (show CA2 Proteins)+) signaling systems, and its levels are limiting for stimulated secretory function in airway goblet cells
Stress-induced mitochondrial hyperfusion (SIMH) is independent of MFN2, BAX/BAK, and prohibitins, but requires L-OPA1, MFN1, and the mitochondrial inner membrane protein SLP-2.
Overexpression of SYTL2 promoted metastatic potential.
SLP2 may play an important role in tumorigenesis of esophageal squamous cell carcinoma.
A high expression level of SLP-2 may be associating with the development of invasion and metastasis in laryngeal squamous cell carcinoma and breast cancer.
Calmodulin (show CALM1 Proteins) suppresses synaptotagmin-2 (show SYT2 Proteins) transcription in cortical neurons
Exophilin4/Slp2-a is specifically expressed in pancreatic alpha cells.
Rab27a (show RAB27A Proteins) recruits Slp2a-hem on vesicular structures in peripheral CTLs and following CTL-target (show CTH Proteins) cell conjugate formation, the Slp2a-hem/Rab27a (show RAB27A Proteins) complex colocalizes with perforin (show PRF1 Proteins)-containing granules at the immunologic synapse
Rab27A/Slp2a expression in limb girdle muscular dystrophy 2B muscle provides a compensatory vesicular trafficking pathway that is able to repair membrane damage in the absence of dysferlin.
Synaptotagmin-like protein 2-a (Slp2-a) contains an N-terminal Slp (show SEPT9 Proteins) homology domain (SHD (show SHD Proteins)) (PMID: 11327731). The SHD (show SHD Proteins) of Slp2-a specifically and directly binds the GTP (show AK3 Proteins)-bound form of Rab27A (show RAB27A Proteins).
The protein encoded by this gene is a synaptotagmin-like protein (SLP) that belongs to a C2 domain-containing protein family. The SLP homology domain (SHD) of this protein has been shown to specifically bind the GTP-bound form of Ras-related protein Rab-27A (RAB27A). This protein plays a role in RAB27A-dependent vesicle trafficking and controls melanosome distribution in the cell periphery. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
, synaptotagmin-like protein 2
, breast cancer-associated antigen SGA-72M
, chromosome 11 synaptotagmin