Surfing on microtubule ends.
A crowd of proteins seems to have gathered around the plus-ends of microtubules. A rapidly expanding group of proteins known as plus-end tracking proteins (+TIPs) have been identified that seem to be able to 'surf' the dynamic ends of microtubules. Microtubule plus-ends exist in multiple conformational and chemical states. In principle, altering this plus-end microenvironment is an appealing way for regulators such as the +TIPS to control microtubule dynamics; however, specific mechanisms are poorly defined. Here, we focus on new findings addressing the underlying mechanisms of plus-end tracking and the mechanisms by which +TIPS control microtubule dynamics. We review the evidence that plus-end-binding and the control of microtubule dynamics are mechanistically linked. We also consider the possibility that, by studying +TIPs, we might learn more about the dynamic structural changes at the microtubule ends that are at the heart of dynamic instability.
Departments of Pediatric Oncology, Dana-Farber Cancer Institute and Pediatric Hematology/Oncology, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.
Pedro
P
Carvalho
Jennifer S
JS
Tirnauer
David
D
Pellman
D000818:Animals; D000072159:Dynactin Complex; D006160:Guanosine Triphosphate / Q000737:chemistry; D006801:Humans; D008869:Microtubule-Associated Proteins / Q000502:physiology; D008870:Microtubules / Q000502:physiology* / Q000648:ultrastructure*; D008954:Models, Biological; D009363:Neoplasm Proteins; D017434:Protein Structure, Tertiary; D014404:Tubulin / Q000737:chemistry; D015003:Yeasts / Q000502:physiology
D000072159:Dynactin Complex; D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; D014404:Tubulin; C076744:cytoplasmic linker protein 170; D006160:Guanosine Triphosphate