High impact information on SEC23IP

• We previously identified and characterized a novel Sec23p-interacting protein, p125, that is only expressed in mammals and exhibits sequence homology with phosphatidic acid-preferring phospholipase A(1) (PA-PLA(1)) [1].
• p125 is localized in endoplasmic reticulum exit sites and involved in their organization [1].
• By using immunofluorescence and electron microscopy, we found that p125 is principally localized in ER exit sites where COPII-coated vesicles are produced [1].
• The N-terminal region of p125 is rich in proline residues, and the central and C-terminal regions exhibit significant homology to phospholipid-modifying proteins, especially phosphatidic acid preferring-phospholipase A1 [2].
• Confocal laser scanning microscopy showed that P125 is a cell membrane bound protein [3].

Anatomical context of SEC23IP

• In the present study we showed that expressed p125 principally colocalizes with p115 and GM130, both of which are involved in vesicle tethering to Golgi membranes [4].
• p125, a mammalian Sec23p-interacting protein, exhibits sequence homology with bovine testis phosphatidic acid-preferring phospholipase A(1) [5].

Other interactions of SEC23IP

• For the correct localization of p125, a region (residues 135-1000) comprising both the proline-rich and phospholipase A(1) homology regions was required [4].

Analytical, diagnostic and therapeutic context of SEC23IP

• Subsequent waveform components could be accounted for by dipoles that were in close proximity to fMRI activations in the following cortical areas: P95 (area MT/V5), P125/N135 (area V1), N150 (transverse parietal sulcus, TPS), N160 (ventral occipital areas VP, V4v, and V4/V8), and N180 (dorsal occipital areas V3A/V7) [6].
• Northern blot studies, using the human P170 cDNA probe, revealed a size of 4.2 kb for the sponge P125 transcript [3].

References