High impact information on SYNJ1

• Moreover, the PIP2 phosphatase activity of native p150 purified from bovine brains is not inhibited by profilin, cofilin, or alpha-actinin, although PLCdelta1 activity is markedly inhibited by these proteins [1].
• All these data suggest that p150 (synaptojanin) hydrolyzes PIP2 bound to actin regulatory proteins, resulting in the rearrangement of actin filaments downstream of tyrosine kinase and Ash/Grb2 [1].
• The expression of p150 in COS 7 cells produces a decrease in the number of actin stress fibers in the center of the cells and causes the cells to become multinuclear [1].
• Furthermore, p150 suppresses actin gelation, which is induced by smooth muscle alpha-actinin [1].
• Here, we show a new mechanism for the hydrolysis of bound PIP2 and the regulation of actin filaments by PIP2 phosphatase (synaptojanin) [1].

Biological context of SYNJ1

• Here, p150 and p65 were affinity-purified with glutathione S-transferase-Ash fusion protein and their partial amino acid sequences were determined [2].
• The p150 has sequence homology with a PIM peptide sequence containing the anti-PIM mAb epitope [3].

Anatomical context of SYNJ1

• All these results suggest that Ash may function as a regulator of synaptic vesicle transport through dynamin, p150 and p65 [2].
• Immunohistochemical staining of rat brain showed p150 and p65 to be localized in a variety of neurons in the cerebellum and hippocampus, with p65 being especially concentrated in the nerve terminal [2].
• By immunoelectron microscopy p150 was subsequently transiently detectable on the sporozoite surface and in the lymphocyte cytosol [3].

Analytical, diagnostic and therapeutic context of SYNJ1

• It was found that p150 and p65 are expressed predominantly in brain, although Ash is widely distributed in all tissues examined by Western blots [2].
• Immunoblotting showed that p150 is also expressed by the schizont stage, but at much lower levels compared to the sporozoite [3].

References