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Biomedical subjects

Richard Newman

Publications and source records attributed to Richard Newman.

5 recordsLinked to original sources
PubMed2003

Recurrent lingual tonsil hyperplasia.

Clinically significant lingual tonsil hypertrophy is a rare entity in children. We describe a child, status postadenotonsillectomy, with recurrent hypertrophy of the lingual tonsil after carbon dioxide laser ablation. Workup was negative for immunodeficiency, cystic fibrosis, and allergies. The findings of examination of multiple biopsy specimens of the tissue suggested follicular hyperplasia, and cytometery showed no evidence of a lymphoproliferative disorder. Empiric treatment with a histamine2-receptor blocker after the sixth carbon dioxide laser ablation prevented lingual tonsil hypertrophy.

Adenoids↗
PubMed2002

VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo.

NSF and p97 are ATPases required for the heterotypic fusion of transport vesicles with their target membranes and the homotypic fusion of organelles. NSF uses ATP hydrolysis to dissociate NSF/SNAPs/SNAREs complexes, separating the v- and t-SNAREs, which are then primed for subsequent rounds of fusion. In contrast, p97 does not dissociate the p97/p47/SNARE complex even in the presence of ATP. Now we have identified a novel essential factor for p97/p47-mediated membrane fusion, named VCIP135 (valosin-containing protein [VCP][p97]/p47 complex-interacting protein, p135), and show that it binds to the p97/p47/syntaxin5 complex and dissociates it via p97 catalyzed ATP hydrolysis. In living cells, VCIP135 and p47 are shown to function in Golgi and ER assembly.

Adenosine Triphosphatases↗
PubMed2002

Sequential SNARE disassembly and GATE-16-GOS-28 complex assembly mediated by distinct NSF activities drives Golgi membrane fusion.

Characterization of mammalian NSF (G274E) and Drosophila NSF (comatose) mutants revealed an evolutionarily conserved NSF activity distinct from ATPase-dependent SNARE disassembly that was essential for Golgi membrane fusion. Analysis of mammalian NSF function during cell-free assembly of Golgi cisternae from mitotic Golgi fragments revealed that NSF disassembles Golgi SNAREs during mitotic Golgi fragmentation. A subsequent ATPase-independent NSF activity restricted to the reassembly phase is essential for membrane fusion. NSF/alpha-SNAP catalyze the binding of GATE-16 to GOS-28, a Golgi v-SNARE, in a manner that requires ATP but not ATP hydrolysis. GATE-16 is essential for NSF-driven Golgi reassembly and precludes GOS-28 from binding to its cognate t-SNARE, syntaxin-5. We suggest that this occurs at the inception of Golgi reassembly to protect the v-SNARE and regulate SNARE function.

Adenosine Triphosphatases↗