Boa constrictor or rattlesnake?

Article Abstract:

Dynamin, a relatively large protein made up of four subunits, may, like all other known GTPases, act as a switch to regulate endocytosis. It appears that GDP-dynamin is recruited to the forming bud, where it forms into rings. The protein's intrinsic GTPase activating protein is activated on completion of a spiral around the neck of the bud, when dynamin tetramers from one end of the spiral stack onto tetramers at the other end. This research has left a number of unanswered questions, including why dynamin changes shape on binding GTP.

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Identification of a specific Ins(1,3,4,5)P4-binding protein as a member of the GAP1 family

Article Abstract:

A protein receptor for inositol 1,3,4,5-tetrakisphosphate, Ins(1,3,4,5)P4, has been purified from stimulated cell tissue that specifically binds Ins(1,4,5)P3. The protein shows a specificity for Ins(1,3,4,5)P4's isomeric configuration and has a high affinity for it. The behavior the protein and its in vitro GAP activity against Ras and Rap indicate a GTPase-activating protein of the GAP1 family while Ras GAP activity is stimulated by Ins(1,3,4,5)P4 and inhibited by phospholipids.

Inositol phosphates

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Ringing necks with dynamin

Article Abstract:

The nature of functioning of Dynamin a large GTPase, essential for endocytosis of surface membranes, is discovered by Jemy E. Hinshaw and Kohye Takei. Their study reveals that Dynamic spontaneously self-assembles itself into rings of coated veside buds. This spontaneous self-assembly enables the Dynamin to interact with membrane vesides and remove them from plasma membrane.

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